| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.53256353 |
| The present report demonstrates a functionally important interaction between RyR 1 and triadin which involves , in part , redox cycling of hyperreactive sulfhydryls in response to channel activation and inactivation . 0.53256353^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.87208801 |
| Skeletal muscle triadin is a sarcoplasmic reticulum ( SR ) membrane protein that had been shown to interact structurally and functionally at the cytoplasmic domain ( amino acid residues 1 47 ) with the ryanodine receptor ( RyR 1 ) , and to undergo phosphorylation by endogenous calmodulin protein kinase ( CaM K 2 ) in isolated terminal cisternae from rabbit fast twitch muscle . 0.87208801^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| In addition , we have used indirect immunofluorescence to localize triadin in relation to the DHPR and the RyR in adult and developing rat skeletal muscle . ^^^ In double immunolabelling experiments of longitudinally oriented adult rat skeletal muscle tissue , triadin specific and RyR specific antibodies resulted in a characteristic striated staining pattern . ^^^ The staining patterns of triadin , RyR , and DHPR antibodies were overlapping throughout development , suggesting that from their earliest appearance the three proteins are components of the triads . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| The subcellular distribution of sarcolemmal dihydropyridine receptor ( DHPR ) and sarcoplasmic reticular triadin and Ca2+ release channel / ryanodine receptor ( RyR ) was determined in adult rabbit ventricle and atrium by double labeling immunofluorescence and laser scanning confocal microscopy . ^^^ In atrium , punctate triadin and RyR specific staining was also observed as spots at the cell periphery and image analysis indicated that the three proteins were co localized at , or just below , the sarcolemma . ^^^ In addition , in the atrial cells triadin and RyR specific staining was observed to form transverse bands in the interior cytoplasm at regularly spaced intervals of approximately 2 micron . ^^^ These data indicate that the DHPR codistributes with triadin and the RyR in rabbit ventricle and atrium , and furthermore suggest that some of the SR Ca2+ release channels in atrium may be activated in the absence of a close association with the DHPR . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Nonreducing sodium dodecyl sulfate polyacrylamide gel electrophoresis of CPM labeled SR protein and Western blot analyses with antiryanodine or antitriadin antibodies reveal that the hyperreactive thiols labeled by CPM under conditions favoring channel closure are localized principally to the RyR protomer and triadin , which constitute < 6 % of the protein in the SR preparation . ^^^ Immunoprecipitation experiments with antiryanodine and antitriadin monoclonal antibodies confirm the location of CPM labeled thiol groups on RyR and triadin , respectively . ^^^ The results indicate that the RyR and triadin contain a small number of highly reactive cysteine residues that selectively conjugate with CPM only when channel closure is favored . ^^^ It is shown that either 1 ) the redox state ( sulfhydryl / disulfide status ) or 2 ) the accessibility of the hyperreactive thiols on the RyR and triadin is determined by the conformational state of the channel . ^^^ Covalent modification of hyperreactive thiols with nanomolar CPM inhibits both Ca ( 2+ ) induced Ca2+ release and the gating activity of single channels reconstituted in bilayers , revealing the essential functional importance of hyperreactive thiols on channel associated proteins . 1 , 4 Naphthoquinone ( 0 . 4 40 pmol / micrograms of protein ) selectively oxidizes hyperreactive thiols on RyR and triadin and releases Ca2+ from SR vesicles , without inhibiting Ca ( 2+ ) ATPase activity . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Triadin , a 95 kD protein isolated from heavy SR , binds both the RyR and DHPR and may thus participate in E C coupling or in interactions responsible for the formation of SR / T tubule junctions . ^^^ Immunofluorescence labeling of normal mouse myotubes shows that the RyR and triadin co aggregate with the DHPR in punctate clusters upon formation of functional junctions . ^^^ Dysgenic myotubes with a deficiency in the alpha 1 subunit of the DHPR show reduced expression and clustering of RyR and triadin ; however , both proteins are still capable of forming clusters and attaining mature cross striated distributions . ^^^ Thus , the molecular organization of the RyR and triadin in the terminal cisternae of SR as well as its association with the T tubules are independent of interactions with the DHPR alpha 1 subunit . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Immunostaining of Western blots showed no evidence of proteolysis of the RyR , the alpha 1 subunit of dihydropyridine receptor ( DHPR ) or triadin in uncoupled fibres . 5 . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Disulphide bonded , high molecular mass clusters of triadin , the junctional protein proposed to mediate interactions in triads , were confirmed to be linked to the RyR . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of mainly triadin and of a high M ( r ) polypeptide , and not of the RyR , is the most remarkable common property . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Since depletion of triadin from solubilized HSR with the column increased the [ 3H ] ryanodine binding activity , we tested a possibility of triadin for a negative regulator of the ryanodine receptor / Ca2+ release channel ( RyR ) . ^^^ Purified triadin not only inhibited [ 3H ] ryanodine binding to the solubilized HSR but also reduced openings of purified RyR incorporated into the planar lipid bilayers . ^^^ These results suggest that triadin inhibits the RyR activity and that RyR is regulated by both triadin and calsequestrin , probably through an interaction between them . ^^^ In this paper , triadin has been first demonstrated to have an inhibitory role in the regulatory mechanism of the RyR . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| The interaction between the DHPR and RyR may be stabilized by other proteins such as triadin ( a SR junctional protein ) and modulated by phosphorylation of the DHPR . . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| The direct molecular interaction of this triadin domain with the ryanodine receptor was confirmed by overlay assay and shown to induce the inhibition of the Ca2+ channel activity of purified RyR in bilayer . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| We studied the targeting of DHPRs and triadin to T tubules and SR in skeletal muscles of dyspedic mouse embryos lacking RyR 1 . ^^^ In dyspedic fibers DHPRs and triadin antibodies stain internal foci of the two proteins ; RyR antibodies are completely negative . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Doxorubicin , 1 , 4 naphthoquinone ( NQ ) , and 1 , 4 benzoquinone ( BQ ) are found to selectively and dose dependently interact with a class of hyperreactive sulfhydryl groups localized on ryanodine sensitive Ca2+ channels [ ryanodine receptor ( RyR ) ] , and its associated protein , triadin , of skeletal type channels . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| In addition to providing further evidence that HCP coenriches with RyR 1 , FKBP 12 , triadin and calsequestrin ( CS ) in sucrose density purified TC vesicles , using specific polyclonal antibody , we show it to be expressed as a single protein species , both in fast twitch and slow twitch fibers , and to identically localize to the 1 band . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Calsequestrin ( CSQ ) is a high capacity Ca ( 2+ ) binding protein in the junctional sarcoplasmic reticulum of striated muscles , and has been shown to regulate the ryanodine receptor ( RyR ) through triadin and junctin . ^^^ Our results suggest that the asp rich region of CSQ could participate in the RyR mediated Ca ( 2+ ) release process by offering a direct binding site to luminal Ca ( 2+ ) as well as triadin . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| We investigated the expression and localization of these proteins as well as intracellular Ca2+ transients during development of human muscle cells cultured aneurally and innervated with rat spinal cord . mRNAs encoding skeletal muscle isoforms of the DHPR alpha 1 subunit ( alpha1S DHPR ) , the RyR , and triadin were scarce in myoblasts and increased remarkably after myotube formation . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Therefore SR surface docking , targeting of triadin and calsequestrin to the junctional SR domains and the structural organization of the two latter proteins are not affected by lack of DHPR and RyR . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Overexpression of junctin led to down regulation of triadin and RyR but to up regulation of dihydropyridine receptor . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| This complex consists of the calcium release channel or ryanodine receptor ( RyR ) , the high capacity calcium binding protein calsequestrin located in the lumen of the junctional SR , and the junctional SR transmembrane proteins triadin 1 and junctin which are hypothesized to anchor calsequestrin to the RyR . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Ca ( 2+ ) storage and release in muscle cells are controlled by a complex of junctional sarcoplasmic reticulum ( jSR ) proteins , that includes the calcium binding protein calsequestrin ( CSQ ) , the Ca ( 2+ ) release channel ( ryanodine receptor or RyR ) and two transmembrane proteins that bind to RyR : junctin ( JNC ) and triadin ( Tr ) . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| In mammalian striated muscles , ryanodine receptor ( RyR ) , triadin , junctin , and calsequestrin form a quaternary complex in the lumen of sarcoplasmic reticulum . ^^^ Here we tested the hypothesis that specific charged amino acids within the luminal portion of RyR mediate its direct interaction with triadin . ^^^ Using in vitro binding assay and site directed mutagenesis , we found that the second intraluminal loop of the skeletal muscle RyR 1 ( amino acids 4860 4917 ) , but not the first intraluminal loop of RyR 1 ( amino acids 4581 4640 ) could bind triadin . ^^^ Using deletional approaches , we showed that a KEKE motif of triadin ( amino acids 200 232 ) is essential for the binding to RyR 1 . ^^^ Because the second intraluminal loop of RyR has been previously shown to contain the ion conducting pore as well as the selectivity filter of the Ca2+ release channel , and Asp 4878 , Asp 4907 , and Glu 4908 residues are predicted to locate at the periphery of the pore assembly of the channel , our data suggest that a physical interaction between RyR 1 and triadin could play an active role in the overall Ca2+ release process of excitation contraction coupling in muscle cells . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| OBJECTIVE : Ca2+ release from the cardiac junctional sarcoplasmic reticulum ( SR ) is regulated by a complex of proteins , including the ryanodine receptor ( RyR ) , calsequestrin ( CSQ ) , junctin ( JCN ) , and triadin 1 ( TRD ) . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| In the present study , we investigated the potential role of the cardiac SR luminal auxiliary proteins calsequestrin ( CSQ ) , triadin 1 , and junctin in forming the luminal calcium sensor for the cardiac RyR . ^^^ When triadin 1 and junctin were added to the luminal side of purified channels , RyR Po increased significantly ; however , the channels still remained unresponsive to changes in luminal [ Ca ] . ^^^ These results suggest that a complex of CSQ , triadin 1 , and junctin confer RyR luminal Ca sensitivity . ^^^ CSQ apparently serves as a luminal Ca sensor that inhibits the channel at low luminal [ Ca ] , whereas triadin 1 and / or junctin may be required to mediate interactions of CSQ with RyR . . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| The polymer is anchored at one end to ryanodine receptor ( RyR ) Ca2+ release channels either via the intrinsic membrane proteins triadin and junctin or by binding directly to the RyR . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| This complex includes proteins that interact with the cytoplasmic part of the RyR directly or indirectly ( e . g . calmodulin ( CaM ) , FK 506 binding proteins , protein kinase A , Ca CaM dependent protein kinase , phosphatases 1 and 2A , mAKAP , spinophilin , PR 130 , sorcin , triadin , junctin , calsequestrin and Homer ) . ^^^ |
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| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| All of these proteins , calsequestrin , RyR , triadin , SERCAs , and sarcalumenin , are involved in calcium uptake , storage , and release . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| In cardiac muscle , junctin forms a quaternary protein complex with the ryanodine receptor ( RyR ) , calsequestrin , and triadin 1 at the luminal face of the junctional sarcoplasmic reticulum ( jSR ) . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| Proteins investigated included : ryanodine receptor , ( RyR ) , dihydropyridine receptor , ( DHPR ) , triadin ( TRI ) , calsequestrin ( CSQ ) , 90 kDa junctional protein ( JSR 90 ) , and fast twitch and slow twitch SR calcium ATPases ( SERCA 1 and SERCA 2 ) . ^^^ |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13061 and P21817 |
Pubmed |
SVM Score :0.0 |
| NA |
|