| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.93753982 |
| Analysis of ZO 1 immunoprecipitation profiles from different cell types , performed under conditions previously demonstrated to maintain interactions between ZO 1 , ZO 2 and p 130 from the MDCK epithelial cell line , show that the proteins which co precipitate with ZO 1 vary with cell type . 0.93753982^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.54760387 |
| We have isolated ZO 2 from MDCK cell monolayers by bulk coimmunoprecipitation with ZO 1 followed by electroelution from preparative SDS PAGE gel slices . 0.54760387^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.71889208 |
| Furthermore , immunoprecipitation experiments revealed that the second PDZ domain of ZO 2 was directly associated with N ZO 1 . 0.71889208^^^ When NH 2 terminal dlg like and COOH terminal non dlg like domains of ZO 2 ( N ZO 2 and C ZO 2 , respectively ) were separately introduced into cultured cells , N ZO 2 was colocalized with endogenous ZO 1 / ZO 2 , i . e . at TJs in epithelial cells and at AJs in non epithelial cells , whereas C ZO 2 was distributed along actin filaments . 0.57257988^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :1.4450517 |
| Exploration of other tight junction protein interactions demonstrated that ZO 2 binds directly to both ZO 1 and occludin . 1.4450517^^^ We utilized in vitro binding assays with purified recombinant proteins and immunoprecipitation analyses to define interactions between ZO 1 , ZO 2 , ZO 3 , occludin , and the actin cytoskeleton . 0.83018754^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.51232061 |
| Although specific roles for ZO 1 at the tight junction are unknown , it is widely assumed that ZO 1 , together with its homologs ZO 2 and ZO 3 , serves as a platform to scaffold various transmembrane and cytoplasmic tight junction proteins . 0.51232061^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| This temperature shift facilitated the tyrosine phosphorylation of the two tight junction proteins , ZO 1 and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Immunoblot analysis revealed that overexpression of claudin 1 increased expression of ZO 1 but not of occludin or ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The localizations of endogenous ZO 1 and another family member , ZO 2 , were disrupted . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Both isoforms of 4 . 1R coprecipitated with proteins that organize tight junctions such as ZO 2 , ZO 1 , and occludin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| ZO 1 , ZO 2 and ZO 3 are tight junction ( TJ ) associated proteins that belong to the MAGUK family . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Cx 45 interacts with the PDZ domains of ZO 1 and ZO 3 , but not ZO 2 , via a short C terminal PDZ binding motif ( SVWI ) . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In contrast , expression levels of ZO 1 , ZO 2 , E cadherin , and beta catenin were not altered by HNF 4alpha . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The tight junction protein ZO 2 contains three PDZ ( PSD 95 / Discs Large / ZO 1 ) domains and an alternatively spliced region . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Coincidently , ZO 1 and another tight junction protein , ZO 2 , become transiently phosphorylated on tyrosine residues , as determined by anti phosphotyrosine immunoblotting . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| These conserved regions are shared among members of the discs large family of proteins that include human p 55 , a membrane protein expressed in erythrocytes , rat PSD 95 / SAP90 , a synapse protein expressed in brain , Drosophila dIg A , a septate junction protein expressed in various epithelia , and human and mouse ZO 1 and canine ZO 2 , two tight junction proteins . dIg A has been shown to act as a tumor suppressor , and the other members may all be involved in signal transduction through specialized membrane domains with highly organized cytoskeletons and thus are potential tumor suppressors . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| A preformed complex containing ZO 1 , ZO 2 , p 130 , as well as 330 and 65 kDa phosphoproteins was detected by coimmunoprecipitation in both the presence and absence of cell cell contact . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Secondly , domain E was expressed in Escherichia coli as a fusion protein with glutathione S transferase , and this fusion protein was shown to be specifically bound to a complex of ZO 1 ( 220 kD ) and ZO 2 ( 160 kD ) among various membrane peripheral proteins . ^^^ In vitro binding analyses using glutathione S transferase fusion proteins of various deletion mutants of domain E narrowed down the sequence necessary for the ZO 1 / ZO 2 association into the domain E358 / 504 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| This superfamily includes the synapse associated protein SAP 97 , a close relative of SAP 90 , the Drosophila tumor suppressor gene product dlg Ap , the mammalian zonula occludens proteins ZO 1 and ZO 2 and the erythrocyte protein p 55 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| This protein is a member of a family of homologs that also includes two proteins found at mammalian tight junctions ( ZO 1 and ZO 2 ) and a protein found at mammalian synaptic junctions ( PSD 95 / SAP90 ) . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| These include the product of the lethal ( 1 ) discs large 1 ( dlgA ) tumor suppressor gene and the zonula occludens proteins ZO 1 , ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In addition , we found a novel phosphoprotein of 130 kD which coimmunoprecipitated with the ZO 1 / ZO 2 complex . ^^^ Although the assembly and sealing of TJs may involve the activation of PKC , the level of phosphorylation of ZO 1 , ZO 2 , and the 130 kD protein did not change after adding Ca2+ or a PKC agonist . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Monoclonal antibody 7H6 reacts with a novel tight junction associated protein distinct from ZO 1 , cingulin and ZO 2 . ^^^ Immunoprecipitation of detergent extracts obtained from metabolically labeled MDCK cells with R26 . 4C coprecipitated a 160 kD protein , which corresponds to ZO 2 , with ZO 1 . ^^^ These results strongly suggest that the 7H6 antibody recognizes a novel tight junction associated protein different from ZO 1 , cingulin and ZO 2 . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Fluorescent staining and western immunoblot analysis of toxin treated cells showed that two tight junctional proteins , ZO 1 and ZO 2 , were depleted in monolayers treated with enzymatically active PE . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| It is the first identified member of a new family of junction associated proteins that includes ZO 1 and ZO 2 , major components of vertebrate tight junctions . ^^^ These results suggest that junctional contacts could play previously unrecognized roles in regulating the growth of epithelial tissues and that ZO 1 and / or ZO 2 may act as tumor suppressor proteins in humans . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The effect on occludin was specific because other tight junction components , ZO 1 , ZO 2 , cingulin , and the adherens junction protein E cadherin , were unaltered by OCC 2 treatment . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In addition , rate zonal centrifugation analysis of a detergent soluble fraction showed an increase in the amount of ZO 1 and ZO 2 in high density fractions following ATP depletion , providing further evidence for association of TJ proteins into a large complex possibly involving the cytoskeleton . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Tight junctions are mediated by molecules such as occludin and its associated ZO 1 and ZO 2 , and adherens junctions are mediated by adhesion molecules such as cadherin and its associated catenins . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Nontransmembrane proteins on the cytosolic leaflet including ZO 1 , ZO 2 , cingulin , 7H6 , and several unidentified phosphoproteins are also believed to be part of the TJ . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Sequence analysis showed that this protein contains three PSD 95 / SAP90 , discs large , ZO 1 ( PDZ ) domains , a src homology ( SH 3 ) domain , and a region similar to guanylate kinase , making it homologous to ZO 1 , ZO 2 , the discs large tumor suppressor gene product of Drosophila , and other members of the MAGUK family of proteins . ^^^ Like ZO 1 and ZO 2 , the novel protein contains a COOH terminal acidic domain and a basic region between the first and second PDZ domains . ^^^ Unlike ZO 1 and ZO 2 , this protein displays a proline rich region between PDZ 2 and PDZ 3 and apparently contains no alternatively spliced domain . ^^^ In vitro affinity analyses demonstrated that recombinant 130 kD protein directly interacts with ZO 1 and the cytoplasmic domain of occludin , but not with ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The intercellular barrier is formed by rows of the transmembrane protein occludin , which is bound on the cytoplasmic surface to ZO 1 and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Subcellular distribution of tight junction associated proteins ( occludin , ZO 1 , ZO 2 ) in rodent skin . ^^^ ZO 1 and ZO 2 are peripheral membrane proteins that are localized at tight junctions in simple epithelial cells and at cadherin based adherens junctions in nonepithelial cells . ^^^ In this study , we investigated the expression and subcellular distribution of occludin , ZO 1 , and ZO 2 in rodent skin . ^^^ Immunoblotting detected all of these molecules in isolated epidermis , but the occludin / ZO 1 ( or occludin / ZO 2 ) ratio was significantly lower than that in cultured simple epithelial cells . ^^^ In the epidermis of adult skin , occludin was concentrated at cell cell borders only in the most superficial zone of the granular cell layer , whereas ZO 1 and ZO 2 were distributed in a much broader zone from the spinous to the granular layers . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| METHODS : Growth curves and transepithelial electrical resistance ( TEER ) were determined , and the cytoskeleton ( actin , alpha tubulin , vimentin ) and TJ ( Zonula occludens proteins ZO 1 , ZO 2 ) were investigated with immunofluorescent methods by confocal laser scanning microscopy ( CLSM ) and digital image restoration . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| ZO 1 has been demonstrated to interact with the transmembrane protein occludin , a second tight junction specific MAGUK , ZO 2 , and F actin , although the nature and functional significance of these interactions is poorly understood . ^^^ To further elucidate the role of ZO 1 within the epithelial tight junction , we have introduced epitope tagged fragments of ZO 1 into cultured MDCK cells and identified domains critical for the interaction with ZO 2 , occludin , and F actin . ^^^ A combination of in vitro and in vivo binding assays indicate that both ZO 2 and occludin interact with specific domains within the N terminal ( MAGUK like ) half of ZO 1 , whereas the unique proline rich C terminal half of ZO 1 cosediments with F actin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Since potential candidates for phosphorylation are the tight junction associated proteins ZO 1 , ZO 2 and ZO 3 , in a previous work we specifically explored these molecules but found no alteration in their phosphorylation pattern . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The tight junction is composed of many proteins and includes three members of the MAGUK ( membrane associated , guanylate kinase like ) protein family : ZO 1 , ZO 2 , and ZO 3 . ^^^ The evolutionary pressure to maintain the sequence of the protein binding domains suggests that homologous domains have different functions in ZO 1 , ZO 2 , and ZO 3 . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Loss of ZO 1 was associated with the altered localization of ZO 2 and occludin . ^^^ In IFN gamma treated cells , ZO 2 and occludin were diffusely distributed , whereas , in control cells , they , along with ZO 1 , were predominantly localized to the tight junctions . ^^^ In contrast to ZO 1 , ZO 2 and occludin did not show any major changes in these parameters . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Peripheral TJ proteins such as zonula occludens 1 ( ZO 1 ) , ZO 2 , and cingulin become extremely insoluble and associate into large macromolecular complexes ( T . ^^^ These changes reversed after ATP repletion , and the movement of insoluble occludin , ZO 1 , and ZO 2 back into the soluble pool was again via a genistein sensitive mechanism . ^^^ Furthermore , during the ATP repletion phase , tyrosine phosphorylation of Triton 10 100 insoluble occludin , which is localized at the junction , as well as ZO 2 , p130 / ZO 3 ( though not ZO 1 ) , and other proteins was evident ; this tyrosine phosphorylation was completely inhibited by genistein . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| These results suggest an important role for cytoplasmic proteins , presumably ZO 1 , ZO 2 , and ZO 3 , in localizing occludin in tight junction fibrils . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Immunofluorescence microscopy and immunoblot analysis showed that activated PMN adhesion to resting monolayers or PMN migration across interleukin 1 treated monolayers does not result in widespread proteolytic loss of TJ proteins ( ZO 1 , ZO 2 , and occludin ) from endothelial borders . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Direct binding of three tight junction associated MAGUKs , ZO 1 , ZO 2 , and ZO 3 , with the COOH termini of claudins . ^^^ ZO 1 , ZO 2 , and ZO 3 , which contain three PDZ domains ( PDZ 1 to 3 ) , are concentrated at tight junctions ( TJs ) in epithelial cells . ^^^ TJ strands are mainly composed of two distinct types of four transmembrane proteins , occludin , and claudins , between which occludin was reported to directly bind to ZO 1 / ZO 2 / ZO 3 . ^^^ However , in occludin deficient intestinal epithelial cells , ZO 1 / ZO 2 / ZO 3 were still recruited to TJs . ^^^ We then examined the possible interactions between ZO 1 / ZO 2 / ZO 3 and claudins . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Cingulin contains globular and coiled coil domains and interacts with ZO 1 , ZO 2 , ZO 3 , and myosin . ^^^ Pull down assays from epithelial , insect cell , and reticulocyte lysates show that an NH ( 2 ) terminal fragment of cingulin ( 1 378 ) interacts in vitro with ZO 1 ( K ( d ) approximately 5 nM ) , ZO 2 , ZO 3 , myosin , and AF 6 , but not with symplekin , and a COOH terminal fragment ( 377 1 , 368 ) interacts with myosin and ZO 3 . ^^^ ZO 1 and ZO 2 immunoprecipitates contain cingulin , suggesting in vivo interactions . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Many ubiquitous molecular constituents of tight junctions have been identified and characterized including claudins , occludin , ZO 1 , ZO 2 , ZO 3 , cingulin , and 7H6 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Cocultures were analyzed for paracellular permeability by measurement of transepithelial electrical resistance ( TER ) and for the tight junction proteins ZO 1 , ZO 2 , occludin , and cingulin by immunocytochemistry and immunoprecipitation . ^^^ Immunoprecipitation of cocultures revealed dephosphorylation of ZO 2 , loss of ZO 1 from ZO 2 , and degradation of ZO 1 but less so of ZO 2 and none of occludin or E cadherin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Tight junction proteins ZO 1 , ZO 2 , and occludin along isolated renal tubules . ^^^ The differential expression of three tight junction proteins , ZO 1 , ZO 2 , and occludin , along isolated rabbit renal tubules is examined in this article . ^^^ METHODS : Microdissected rabbit renal tubules were processed for immunofluorescence detection of ZO 1 , ZO 2 , and occludin . ^^^ CONCLUSIONS : The distribution of ZO 1 , ZO 2 , and occludin follows the increase in junction complexity encountered in renal tubules . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Human gastric epithelial cells were isolated from samples of human gastric lining and immortalized with simian virus 40 ( SV 40 ) to generate the stable human gastric epithelial cell line `` JOK l . ' ' These cells express conventional epithelial markers ( vimentin , cytokeratin 18 , occludin , N and E cadherins , beta catenin , ZO 1 , ZO 2 , mucin , epithelial specific antigen ) as well as SV 40 large T antigen . ^^^ In contrast , the kidney epithelial cell line `` MDCK ' ' also expresses several epithelial markers ( vimentin , cytokeratin 18 , occludin , N and E cadherin , beta catenin , ZO 1 , ZO 2 , epithelial specific antigen ) , but does not express mucin , or large T antigen . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Removal of calcium from the culture media of the epithelial cells resulted in disruption of the TJs , characterised by a loss of membrane association of the TJ associated proteins occludin , ZO 1 and ZO 2 , by a loss of TJ strands , by a marked decrease in the transepithelial electrical resistance and by a dramatic increase in the transepithelial permeability to tracers . ^^^ The association of occludin , ZO 1 and ZO 2 with the actin cytoskeleton is not affected . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Human and Xenopus cingulin heads are only 33 % identical , yet a human cingulin N terminal fragment still interacts with canine ZO 1 and ZO 2 in vitro . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The tight junction components ZO 1 , ZO 2 , endogenous ZO 3 , and occludin were mislocalized during the early stages of tight junction assembly . ^^^ NZO 3 expression did not alter expression levels of ZO 1 , ZO 2 , endogenous ZO 3 , occludin , or E cadherin ; however , the amount of Triton 10 100 soluble , signaling active beta catenin was increased in NZO 3 expressing cells during junction assembly . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| PURPOSE : To investigate the expression and cellular distribution of putative tight junction ( TJ ) proteins occludin , ZO 1 , ZO 2 , and claudin 1 in rat corneal epithelium and alterations of TJs in cultured human corneal epithelial cells in response to lipopolysaccharide ( LPS ) challenge . ^^^ METHODS : Immunohistochemistry was used to determine tissue distribution of occludin , ZO 1 , ZO 2 , and claudin 1 in the rat cornea . ^^^ Immunocytochemistry and immunoblotting were used to assess alteration in the levels and localization of TJ associated proteins occludin , ZO 1 , and ZO 2 in LPS treated THCE cells . ^^^ RESULTS : Occludin , ZO 1 , and ZO 2 were found at the cell borders of the superficial layer , whereas claudin 1 was localized mainly in the basal and wing cell layers of rat corneal epithelium . ^^^ Specifically , LPS challenge resulted in a decrease in the levels of ZO 1 and ZO 2 compared with untreated cells . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| IL 15 mediated up regulation of ZO 1 and ZO 2 expression was independent of the IL 2Rbeta subunit , whereas the phosphorylation of occludin and enhanced membrane association of claudin 1 and claudin 2 by IL 15 required the presence of the IL 2Rbeta subunit . ^^^ Recruitment of claudins and hyperphosphorylated occludin into tight junctions resulted in a more marked induction of tight junction formation in intestinal epithelial cells than the up regulation of ZO 1 and ZO 2 by itself . ^^^ The regulation of the intestinal epithelial barrier function by IL 15 involves IL 2Rbeta dependent and independent signaling pathways leading to the recruitment of claudins , hyperphosphorylated occludin , ZO 1 , and ZO 2 into the tight junctional protein complex . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| We show that these compounds promote the differentiation of human colon carcinoma SW 480 cells expressing vitamin D receptors ( VDRs ) ( SW 480 ADH ) but not that of a malignant subline ( SW 480 R ) or metastasic derivative ( SW 620 ) cells lacking VDR . 1alpha , 25 ( OH ) 2D ( 3 ) induced the expression of E cadherin and other adhesion proteins ( occludin , Zonula occludens [ ZO ] 1 , ZO 2 , vinculin ) and promoted the translocation of beta catenin , plakoglobin , and ZO 1 from the nucleus to the plasma membrane . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| We have previously found that several MAGUKs , including those of the tight ( ZO 1 , ZO 2 , and ZO 3 ) and septate junction ( tamou and Dlg ) , contain one or two nuclear sorting signals located at their first PDZ and GK domains . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Both integral ( claudin 1 and occludin ) and membrane associated zonula occluden 1 and 2 ( ZO 1 and ZO 2 ) proteins combine to form these TJ complexes that are anchored to the cytoskeletal architecture ( actin ) . ^^^ Furthermore , immunofluorescence studies showed alterations in occludin , ZO 1 , and ZO 2 protein localization during hypoxia and posthypoxic reoxygenation that correlate with the observed changes in BBMEC permeability . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| MAGI 1 , ZO 1 , and ZO 2 all colocalize in nonpolarized epithelial cells , suggesting that they form a preassembled complex that is incorporated into the tight junction upon polarization . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In these studies , we constructed Galpha glutathione S transferase ( GST ) fusion proteins and tested for interactions with [ ( 35 ) S ] methionine labeled in vitro translated ZO 1 and ZO 2 . ^^^ Only Galpha ( 12 ) directly interacted with in vitro translated ZO 1 and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| S . flexneri serotype 2a and 5 , but not the non invasive Escherichia coli strain F 18 , share the ability to regulate expression of ZO 1 , ZO 2 , E cadherin and to dephosphorylate occludin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The PLC gamma inhibitor , 3 NC , but not the inactive analog , 7 OH 3 NC , caused hyperphosphorylation of the tight junction proteins , occludin , ZO 1 , and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In the present work we demonstrate that heterotypic TJs in mixed monolayers of MDCK cells with a different cell type ( LLC PK 1 ) are true TJs through several criteria , such as TER , the ability to stop the membrane diffusion of fluorescent sphingomyelin from the apical to the lateral domain , the presence of ZO 1 , ZO 2 , occludin , claudin 1 and claudin 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| To elucidate mechanisms of endothelial cell ( EC ) dysfunction in CNS inflammatory responses and beneficial effects of interferon beta ( IFN gamma ) in multiple sclerosis ( MS ) , we analyzed effects of individual and combinations of soluble inflammatory mediators on the intracellular localization of the EC tight junction associated molecules zonula occludens 1 and 2 ( ZO 1 and ZO 2 ) in human brain ECs . ^^^ The cytoplasm in the majority of cells in control EC cultures was clear ; ZO 1 and ZO 2 were localized peripherally near sites of cell contact and associated with submembranous cytoplasmic filaments . ^^^ H2O2 induced reversible time and concentration dependent translocation of ZO 1 and ZO 2 to a random distribution within EC cytoplasm and retraction of EC borders . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| This process is accompanied by increased junctional localization and cytoskeletal association of the adherens junctional plakoglobin and the tight junction associated proteins ZO 1 , ZO 2 , and occludin . ^^^ Plakoglobin , ZO 1 , ZO 2 , and occludin showed increased junctional localization when 10T1 / 2 cells were present . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Zonula occludens proteins ( ZOPs ) , currently comprising ZO 1 , ZO 2 , and ZO 3 , belong to the family of membrane associated guanylate kinase homologue ( MAGUK ) proteins that are involved in the organization of epithelial and endothelial intercellular junctions . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Finally , we show that the incisures also contain four other PDZ proteins that are found in epithelial tight junctions , including three membrane associated guanylate kinase proteins ( membrane associated guanylate kinase inverted 2 , ZO 1 , and ZO 2 ) and the adaptor protein Par 3 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Dynamic assembly of tight junction associated proteins ZO 1 , ZO 2 , ZO 3 and occludin during mouse tooth development . ^^^ In order to address these questions , we have studied the distribution pattern of the tight junction associated proteins ZO 1 , ZO 2 , ZO 3 and occludin in the developing mouse tooth as a model . ^^^ The occurrence and relation during tooth development of tight junction proteins ZO 1 , ZO 2 and occludin , but not ZO 3 , suggests a combinatory assembly in tooth morphogenesis and cell differentiation . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Many ubiquitous molecular tight junction components have been identified and characterized including claudins , occludin , ZO 1 , ZO 2 , ZO 3 , cingulin and 7H6 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of occludin attenuates its interactions with ZO 1 , ZO 2 , and ZO 3 . ^^^ While the homotypic interaction of extracellular loops of occludin appears to determine the barrier function of tight junction , the intracellular C terminal tail , C occludin , interacts with other tight junction proteins such as ZO 1 , ZO 2 , and ZO 3 and with the actin filaments of cytoskeleton . ^^^ The effect of tyrosine phosphorylation of C occludin on its ability to bind ZO 1 , ZO 2 , ZO 3 , and F actin was evaluated . ^^^ Results show that the amounts of ZO 1 , ZO 2 , and ZO 3 bound to tyrosine phosphorylated C occludin were several fold less than the amounts bound to non phosphorylated C occludin . ^^^ These results demonstrate that tyrosine phosphorylation of occludin reduces its ability to bind ZO 1 , ZO 2 , and ZO 3 , but not F actin . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Expression of the various genes throughout human preimplantation development showed differing levels of sensitivity of detection ; these genes included claudin 1 , occludin ( TM4+ and TM 4 isoforms ) , ZO 1 ( ZO 1alpha+ and ZO 1alpha isoforms ) , ZO 2 and JAM ( junction adhesion molecule ) , and the desmosome junction gene , DSC 2 ( desmocollin 2 ) . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Calpeptin treatment of MDCK cells resulted in a displacement of zonula occludens 1 ( ZO 1 ) and occludin from cell cell junctions and a loss of phosphotyrosine on ZO 1 and ZO 2 , without any detectable effect on tight junction permeability . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| We showed here that cAMP increased gene expression of claudin 5 and decreased that of claudin 1 in porcine blood brain barrier endothelial cells via protein kinase A ( PKA ) independent and dependent pathways , respectively . cAMP also enhanced immunoreactivity of claudin 5 along cell borders and in the cytoplasm , reorganized actin filaments , and altered signals of claudin 5 , occludin , ZO 1 , and ZO 2 along cell boundaries from zipperlike to linear patterns . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| MCP 1 induces reorganization of actin cytoskeleton ( stress fiber formation ) and redistribution of tight junction proteins , ZO 1 , ZO 2 occludin and claudin 5 , from the Triton 10 100 soluble to the Triton 10 100 insoluble fractions . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Strikingly , opening of the endothelial TJs was not accompanied by any visible change in the molecular composition of endothelial TJs as junctional localization of the TJ associated proteins claudin 3 , claudin 5 , occludin , ZO 1 or ZO 2 or the adherens junction associated proteins beta catenin or p120cas did not change . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : Three related MAGUK proteins , ZO 1 , ZO 2 and ZO 3 , are concentrated at the cytoplasmic surface of tight junctions . ^^^ However , in contrast to ZO 1 / ZO 2 , our knowledge of the expression and distribution of ZO 3 is still fragmentary , partly due to a lack of antibodies that specifically distinguish ZO 3 from ZO 1 and ZO 2 . ^^^ The immunofluorescence signals obtained with these antibodies completely disappeared from ZO 1 / ZO 2 positive tight junctions in the liver of ZO 3 deficient mice , indicating that the antibodies can be used to localize ZO 3 in various tissues by immunofluorescence microscopy . ^^^ Immunofluorescence microscopy with these antibodies revealed that ZO 3 was concentrated at tight junctions in various types of epithelium , but not in endothelium or at cadherin based cell cell adhesion sites ( spot adherens junctions of fibroblasts and intercalated discs of cardiac muscle cells ) , where ZO 1 and ZO 2 are concentrated . ^^^ CONCLUSIONS : We conclude that ZO 3 is expressed in a more epithelium specific manner than ZO 1 and ZO 2 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Paralleling hypoxia and VEGF induced permeability changes , localization of the tight junction proteins occludin , zonula occludens 1 ( ZO 1 ) , and ZO 2 along the cell membrane changed from a continuous to a more discontinuous expression pattern during hypoxia . ^^^ In particular , localization of ZO 1 and ZO 2 expression moved from the cell membrane to the cytoplasm and nucleus whereas occludin expression remained at the cell membrane . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In well polarized epithelial cells , closely related ZO 1 and ZO 2 are thought to function as scaffold proteins at tight junctions ( TJs ) . ^^^ In good agreement , by immunofluorescence microscopy , most TJ proteins including claudins and occludin appeared to be normally concentrated at TJs of ZO 1 / cells with the exception that a ZO 1 deficiency significantly up or down regulated the recruitment of ZO 2 and cingulin , another TJ scaffold protein , respectively , to TJs . ^^^ This retardation as well as the disappearance of cingulin were rescued completely by exogenous ZO 1 but not by ZO 2 expression . ^^^ Quantitative evaluation of ZO 1 / ZO 2 expression levels led to the conclusion that ZO 1 and ZO 2 would function redundantly to some extent in junction formation / epithelial polarization but that they are not functionally identical . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| RT PCR was used to examine the expression of cytoplasmic proteins associated with the tight junctions , ZO 1 ( zonula occludens 1 ) and ZO 2 ( zonula occludens 2 ) . ^^^ RT PCR results showed that the expressions of ZO 1 and ZO 2 were significantly increased after MP treatment , consistent with improved epithelial barrier function . ^^^ The effect of MP on ZO 1 and ZO 2 was mimicked by Ligustrazine and the ligustrazine induced ISC was also blocked by basolateral application of bumetanide and apical addition of diphenylamine 2 , 2 ' dicarboxylic acid or glibenclamide , and reduced by a removal of extracellular Cl . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| In hetero and homozygous ( + / and / ) embryoid bodies , immunoblotting revealed a Triton soluble , truncated form of cingulin , increased levels of the tight junction proteins ZO 2 , occludin , claudin 6 and Lfc , and decreased levels of ZO 1 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Interactions with ZO 1 and ZO 2 , in particular , may mediate recruitment of ARVCF to the plasma membrane and the nucleus , respectively , possibly in response to cell cell adhesion cues . . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The aim of this study was to investigate the expression of Zonula Occludens ( ZO ) proteins ZO 1 , ZO 2 and ZO 3 , and MUPP 1 ( multi PDZ domain protein 1 ) , peripheral / plaque proteins that function in maintaining tight junction integrity and in transducing regulatory signalling events in patients with primary breast cancer . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| We find that the HDAC inhibitor sodium butyrate significantly up regulates the protein levels of cingulin , ZO 1 , and ZO 2 in Rat 1 fibroblasts , cingulin in COS 7 cells , and cingulin and occludin in HeLa cells . ^^^ Levels of mRNA for cingulin , ZO 1 , and ZO 2 are also increased in sodium butyrate treated Rat 1 fibroblasts . ^^^ Up regulation of TJ proteins by sodium butyrate is linked to the ability of sodium butyrate to inhibit HDAC activity , because suberoylanilide hydroxamic acid , a HDAC inhibitor of a different structural class , also up regulates cingulin , ZO 1 , and ZO 2 expression in Rat 1 fibroblasts . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| At the cellular level , MCP 1 causes alteration of tight junction ( TJ ) proteins in endothelial cells ( redistribution of TJ proteins determined by Western blotting and loss of immunostaining for occludin , claudin 5 , ZO 1 , ZO 2 ) . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Also , gp 120 proteins caused disruption and downregulation of the tight junction proteins ZO 1 , ZO 2 , and occludin in these cells . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| MS / MS analysis of tryptic fragments yielded several proteins including zona occludens 1 ( ZO 1 ) , a structural protein previously identified to interact with Cx 43 , and ZO 2 , a potential novel interacting partner . ^^^ Immunofluorescence studies indicate that both ZO 1 and ZO 2 can co localize with Cx 43 within the plasma membrane at apparent gap junctional structures . ^^^ We examined Cx 43 interaction with ZO 1 and ZO 2 at different stages of the cell cycle and found that Cx 43 had a strong preference for interaction with ZO 1 during G 0 , whereas ZO 2 interaction occurred approximately equally during G 0 and S phases . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The C terminus can also bind to the scaffolding proteins ZO 1 , ZO 2 , ZO 3 , cingulin , the membrane trafficking protein VAP 33 , and the cytoskeletal protein F actin , suggesting an important role for this domain . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| We herein show that not only ZO 1 and ZO 2 , but also ZO 3 , junctional adhesion molecule ( JAM ) B , JAM C and cell polarity proteins PAR 3 , PAR 6 and atypical protein kinase C ( aPKC ) accumulate at primordial adherens junctions in undifferentiated F 9 cells . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| Paracellular permeability changes by H2O2 correlated to changes of the localization of the tight junction ( TJ ) proteins occludin , zonula occludens 1 ( ZO 1 ) , and zonula occludens 2 ( ZO 2 ) which were prevented by blocking the p44 / p42 MAP kinase activation . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| However , the molecular functions of ZO 1 and related proteins such as ZO 2 and ZO 3 have remained unclear . ^^^ Depletion of ZO 2 , cingulin , or occludin , proteins that can interact with ZO 1 , had no discernible effects on tight junctions . ^^^ These data reveal an unexpected function for the SH 3 domain of ZO 1 in regulating tight junction assembly in epithelial cells and show that cingulin , occludin , or ZO 2 are not limiting for junction assembly in MDCK monolayers . . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The present study used cultured brain endothelial cells to examine the signaling networks involved in the redistribution of TJ proteins ( occludin , ZO 1 , ZO 2 , claudin 5 ) by CCL 2 . ^^^ The CCL 2 induced alterations in the brain endothelial barrier were associated with de novo Ser / Thr phosphorylation of occludin , ZO 1 , ZO 2 , and claudin 5 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| It forms complexes with the cytoplasmic proteins ZO 1 , ZO 2 and ZO 3 . ^^^ This domain , as expressed in a bacterial system or isolated from native cellular occludin , maintains its ability to bind ZO 1 and ZO 2 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| TJ proteins identified include transmembrane proteins ; occludin and claudin , and cytoplasmic plaque proteins ; ZO 1 , ZO 2 , ZO 3 , cingulin , and 7H6 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| The transmembrane tight junction proteins occludin , claudin 1 and claudin 5 , as well as the cytoplasmic accessory proteins ZO 1 and ZO 2 displayed a continuous distribution at cell boundaries . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| While molecular expression of junctional adhesion molecule ( JAM ) , ZO 2 , ZO 3 , claudin 2 and claudin 3 were unaltered , ZO 1 , occludin , and claudin 4 were all up regulated ( 1 . 6 , 1 . 6 , 2 . 4 fold , respectively ; P < 0 . 001 0 . 01 ) and claudin 1 down regulated ( 2 . 5 fold ; P < 0 . 05 ) by trans 10 , cis 12 CLA , which may underpin its effects on tight junction function and paracellular Ca transport . ^^^ |
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| Interacting proteins: Q9UDY2 and Q07157 |
Pubmed |
SVM Score :0.0 |
| ZO 1 and ZO 2 independently determine where claudins are polymerized in tight junction strand formation . ^^^ ZO 1 and ZO 2 are major PDZ domain containing TJ proteins and bind directly to claudins , yet their functional roles are poorly understood . ^^^ We established cultured epithelial cells ( 1 ( ko ) / 2 ( kd ) ) in which the expression of ZO 1 / ZO 2 was suppressed by homologous recombination and RNA interference , respectively . ^^^ When exogenously expressed in 1 ( ko ) / 2 ( kd ) cells , ZO 1 and ZO 2 were recruited to junctional areas where claudins were polymerized , but truncated ZO 1 ( NZO 1 ) containing only domains PDZ 1 3 was not . ^^^ These findings indicate that ZO 1 and ZO 2 can independently determine whether and where claudins are polymerized . . ^^^ |
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