| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.59013006 |
| In this study , we show that PINCH co localizes with ILK in both focal adhesions and fibrillar adhesions . 0.59013006^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.67835613 |
| We show here that ILK forms a complex with PINCH and CH ILKBP in primary mesangial cells , which are co clustered at fibrillar adhesions , sites that are involved in fibronectin matrix deposition . 0.67835613^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Characterization of PINCH 2 , a new focal adhesion protein that regulates the PINCH 1 ILK interaction , cell spreading , and migration . ^^^ Importantly , the PINCH 2 ILK and PINCH 1 ILK interactions are mutually exclusive . ^^^ Overexpression of PINCH 2 significantly inhibited the PINCH 1 ILK interaction and reduced cell spreading and migration . ^^^ These results identify a novel nuclear and focal adhesion protein that associates with ILK and reveals an important role of PINCH 2 in the regulation of the PINCH 1 ILK interaction , cell shape change , and migration . . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| PINCH 1 is an obligate partner of integrin linked kinase ( ILK ) functioning in cell shape modulation , motility , and survival . ^^^ PINCH 1 is a widely expressed focal adhesion protein that forms a ternary complex with integrin linked kinase ( ILK ) and CH ILKBP / actopaxin / alpha parvin ( abbreviated as alpha parvin herein ) . ^^^ We have used RNA interference , a powerful approach of reverse genetics , to investigate the functions of PINCH 1 and ILK in human cells . ^^^ First , PINCH 1 and ILK , but not alpha parvin , are essential for prompt cell spreading and motility . ^^^ Second , PINCH 1 and ILK , like alpha parvin , are crucial for cell survival . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Loss of PINCH 1 or ILK , to which alpha and beta parvin bind , significantly reduced the activation of Rac , a key signaling event that controls lamellipodium formation and cell spreading . ^^^ Overexpression of beta parvin , however , was insufficient for stimulation of Rac activation or lamellipodium formation , although it was sufficient for promotion of apoptosis , another important cellular process that is regulated by PINCH 1 , ILK , and alpha parvin . ^^^ These results identify Rac as a downstream target of PINCH 1 , ILK , and parvin . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| PINCH 1 , an adaptor protein composed of five LIM domains , mediates protein protein interactions and functions as a component of the integrin integrin linked kinase ( ILK ) complex . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| With the use of an inducible podocyte differentiation system , it was found that the cellular levels of PINCH 1 , integrin linked kinase ( ILK ) , and alpha parvin , cytoplasmic components of cell extracellular matrix adhesions , were significantly increased during podocyte differentiation . ^^^ Concomitantly , an increased amount of the PINCH 1 ILK alpha parvin complex was detected in the differentiated , foot process containing podocytes . ^^^ Overexpression of the PINCH 1 binding ankyrin repeat domain of ILK but not that of a PINCH 1 binding defective mutant form of the ankyrin domain effectively inhibited the formation of the PINCH 1 ILK alpha parvin complex . ^^^ Disruption of the PINCH 1 ILK alpha parvin complex significantly reduced the podocyte matrix adhesion and foot process formation . ^^^ Furthermore , a marked increase of apoptosis in the podocytes in which the assembly of the PINCH 1 ILK alpha parvin complex was compromised was detected . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| PINCH 1 , a widely expressed protein consisting of five LIM domains and a C terminal tail , is an essential focal adhesion protein with multiple functions including regulation of the integrin linked kinase ( ILK ) level , cell shape , and survival signaling . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| PINCH 1 is composed of 5 LIM domains , binds integrin linked kinase ( ILK ) and locates to integrin mediated adhesion sites . ^^^ Similar to mice lacking beta 1 integrin or Ilk , loss of PINCH 1 arrested development at the peri implantation stage . ^^^ In contrast to beta 1 integrin or Ilk mutants , however , disruption of the PINCH 1 gene produced implantation chambers with visible cell clumps even at embryonic day 9 . 5 . ^^^ In order to define the phenotype leading to the peri implantation lethality we made PINCH 1 null EBs and found similar but also additional defects not observed in beta 1 integrin or Ilk mutant EBs . ^^^ Although ILK and PINCH 1 were shown to be involved in the phosphorylation of serine 473 of PKB / Akt , immunostaining with specific antibodies revealed no apparent alteration of PKB / Akt phosphorylation in PINCH 1 deficient EBs . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| In this article , 1 discuss recent evidence that indicates that PINCH 1 and integrin linked kinase ( ILK ) , which form a tight complex in cells , serve as one of the hubs in the integrin actin network . ^^^ Consequently , loss of the PINCH 1 ILK complex is disastrous for embryogenesis in vertebrates and invertebrates . ^^^ Dissecting the interactions and functions that are mediated by the PINCH 1 ILK complex presents an exciting challenge and an opportunity to unravel the structure and functions of the integrin actin network . . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| A complex of PARVA with ILK and the LIM protein PINCH 1 is critical for cell survival in a variety of cells , including certain cancer cells , kidney podocytes and cardiac myocytes . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| PINCH , an ILK binding protein , exhibited a similar expression pattern in the skin . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| We report here that PINCH is a binding protein for integrin linked kinase ( ILK ) , an intracellular serine / threonine protein kinase that plays important roles in the cell adhesion , growth factor , and Wnt signaling pathways . ^^^ The interaction between ILK and PINCH has been consistently observed under a variety of experimental conditions . ^^^ Furthermore , ILK , but not vinculin or focal adhesion kinase , has been coisolated with PINCH from mammalian cells by immunoaffinity chromatography , indicating that PINCH and ILK associate with each other in vivo . ^^^ The PINCH ILK interaction is mediated by the N terminal most LIM domain ( LIM 1 , residues 1 to 70 ) of PINCH and multiple ankyrin ( ANK ) repeats located within the N terminal domain ( residues 1 to 163 ) of ILK . ^^^ Additionally , biochemical studies indicate that ILK , through the interaction with PINCH , is capable of forming a ternary complex with Nck 2 , an SH2 / SH3 containing adapter protein implicated in growth factor receptor kinase and small GTPase signaling pathways . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| ILK binds to PINCH through the N terminal ankyrin ( ANK ) repeat domain and the PINCH binding is crucial for focal adhesion localization of ILK . ^^^ The ILK PINCH interaction also connects ILK to Nck 2 , an SH 2 SH3 containing adaptor protein that interacts with components of growth factor and small GTPase signaling pathways . ^^^ Recent genetic studies in Drosophila melanogaster and Caenorhabditis elegans have shown that lack of expression of ILK or PINCH results in phenotypes resembling those of integrin null mutants , which demonstrates that ILK and PINCH are indispensable for integrin function during embryonic development . . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| In previous studies , we have identified PINCH , a protein consisting of five LIM domains , as an ILK binding protein . ^^^ We demonstrate in this study that the ILK PINCH interaction requires the N terminal most ANK repeat ( ANK 1 ) of ILK and one ( the C terminal ) of the two zinc binding modules within the LIM 1 domain of PINCH . ^^^ The ILK ANK repeats domain , which is capable of interacting with PINCH in vitro , could also form a complex with PINCH in vivo . ^^^ The PINCH binding defective ANK 1 deletion ILK mutant , unlike the wild type ILK , was unable to localize and cluster in focal adhesions , suggesting that the interaction with PINCH is necessary for focal adhesion localization and clustering of ILK . ^^^ These results suggest that focal adhesions are a major subcellular compartment where ILK functions in intracellular signal transduction , and provide important evidence for a critical role of PINCH and integrins in regulating ILK cellular function . . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| The LIM 1 domain of PINCH interacts with integrin linked kinase ( ILK ) , thereby mediating focal adhesions via a specific integrin / ILK signaling pathway . ^^^ We have solved the NMR structure of the PINCH LIM 1 domain and characterized its binding to ILK . ^^^ Gel filtration and NMR experiments demonstrated a 1 : 1 complex between PINCH LIM 1 and the ankyrin repeat domain of ILK . ^^^ A chemical shift mapping experiment identified regions in PINCH LIM 1 that are important for interaction with ILK . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| CH ILKBP , ILK , and PINCH , a FA protein that binds the NH ( 2 ) terminal domain of ILK , form a complex in cells . ^^^ These findings reveal a novel CH ILKBP ILK PINCH complex and provide important evidence for a crucial role of this complex in the regulation of cell adhesion and cytoskeleton organization . . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Assembly of the PINCH ILK CH ILKBP complex precedes and is essential for localization of each component to cell matrix adhesion sites . ^^^ PINCH , integrin linked kinase ( ILK ) and calponin homology containing ILK binding protein ( CH ILKBP ) form a ternary complex that plays crucial roles at cell extracellular matrix adhesion sites . ^^^ Three dimensional structure based point mutations identified specific PINCH and ILK sites that mediate the complex formation . ^^^ Analyses of the binding defective point mutants revealed that the assembly of the PINCH ILK CH ILKBP complex is essential for their localization to cell extracellular matrix adhesion sites . ^^^ The formation of the PINCH ILK CH ILKBP complex precedes integrin mediated cell adhesion and spreading . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Particularly interesting new cysteine histidine rich protein ( PINCH ) is a double zinc finger domain ( LIM ) only adapter protein that functions to recruit the integrin linked kinase ( ILK ) to sites of integrin activation . ^^^ Genetic studies have shown that PINCH and ILK are required for integrin signaling . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| We demonstrate that Drosophila PINCH and ILK are complexed in vivo and are coincident at the integrin rich muscle attachment sites in embryonic muscle . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Although many intracellular proteins have been implicated in these processes , a new paradigm is emerging from biochemical and genetic studies that implicates integrin linked kinase ( ILK ) and its interacting proteins , such as CH ILKBP ( alpha parvin ) , paxillin , and PINCH in coupling integrins to the actin cytoskeleton and signaling complexes . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| We found that thymosin beta 4 formed a functional complex with PINCH and integrin linked kinase ( ILK ) , resulting in activation of the survival kinase Akt ( also known as protein kinase B ) . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| Next , we will focus on one of the recently discovered cell ECM adhesion protein complexes consisting of PINCH , integrin linked kinase ( ILK ) , and Parvin and use it as an example to illustrate the molecular basis underlying the assembly and functions of cell ECM adhesions . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| They consist of three members ( alpha , beta , and gamma parvin ) , form a functional complex with integrin linked kinase ( ILK ) and PINCH , and link integrins to the actin cytoskeleton . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| ILK , PINCH and parvin : the tIPP of integrin signalling . ^^^ The ternary complex of integrin linked kinase ( ILK ) , PINCH and parvin functions as a signalling platform for integrins by interfacing with the actin cytoskeleton and many diverse signalling pathways . ^^^ |
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| Interacting proteins: P48059 and Q13418 |
Pubmed |
SVM Score :0.0 |
| NA |
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