Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane - PubMed (original) (raw)
. 1997 Sep 12;272(37):23389-97.
doi: 10.1074/jbc.272.37.23389.
Affiliations
- PMID: 9287354
- DOI: 10.1074/jbc.272.37.23389
Free article
Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
L Zhang et al. J Biol Chem. 1997.
Free article
Abstract
Several key proteins have been localized to junctional sarcoplasmic reticulum which are important for Ca2+ release. These include the ryanodine receptor, triadin, and calsequestrin, which may associate into a stable complex at the junctional membrane. We recently purified and cloned a fourth component of this complex, junctin, which exhibits homology with triadin and is the major 125I-calsequestrin-binding protein detected in cardiac sarcoplasmic reticulum vesicles (Jones, L. R., Zhang, L., Sanborn, K., Jorgensen, A. O., and Kelley, J. (1995) J. Biol. Chem. 270, 30787-30796). In the present study, we have examined the binding interactions between the cardiac forms of these four proteins with emphasis placed on the role of junctin. By a combination of approaches including calsequestrin-affinity chromatography, filter overlay, immunoprecipitation assays, and fusion protein binding analyses, we find that junctin binds directly to calsequestrin, triadin, and the ryanodine receptor. This binding interaction is localized to the lumenal domain of junctin, which is highly enriched in charged amino acids organized into "KEKE" motifs. KEKE repeats are also found in the common lumenal domain of triadin, which likewise is capable of binding to calsequestrin and the ryanodine receptor (Guo, W., and Campbell, K. P. (1995) J. Biol. Chem. 270, 9027-9030). It appears that junctin and triadin interact directly in the junctional sarcoplasmic reticulum membrane and stabilize a complex that anchors calsequestrin to the ryanodine receptor. Taken together, these results suggest that junctin, calsequestrin, triadin, and the ryanodine receptor form a quaternary complex that may be required for normal operation of Ca2+ release.
Similar articles
- The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.
Györke I, Hester N, Jones LR, Györke S. Györke I, et al. Biophys J. 2004 Apr;86(4):2121-8. doi: 10.1016/S0006-3495(04)74271-X. Biophys J. 2004. PMID: 15041652 Free PMC article. - Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.
Wei L, Gallant EM, Dulhunty AF, Beard NA. Wei L, et al. Int J Biochem Cell Biol. 2009 Nov;41(11):2214-24. doi: 10.1016/j.biocel.2009.04.017. Epub 2009 May 4. Int J Biochem Cell Biol. 2009. PMID: 19398037 Free PMC article. - Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin.
Beard NA, Wei L, Cheung SN, Kimura T, Varsányi M, Dulhunty AF. Beard NA, et al. Cell Calcium. 2008 Oct;44(4):363-73. doi: 10.1016/j.ceca.2008.01.005. Cell Calcium. 2008. PMID: 19230141 - Calsequestrin and the calcium release channel of skeletal and cardiac muscle.
Beard NA, Laver DR, Dulhunty AF. Beard NA, et al. Prog Biophys Mol Biol. 2004 May;85(1):33-69. doi: 10.1016/j.pbiomolbio.2003.07.001. Prog Biophys Mol Biol. 2004. PMID: 15050380 Review. - Control of muscle ryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen.
Beard NA, Wei L, Dulhunty AF. Beard NA, et al. Clin Exp Pharmacol Physiol. 2009 Mar;36(3):340-5. doi: 10.1111/j.1440-1681.2008.05094.x. Clin Exp Pharmacol Physiol. 2009. PMID: 19278523 Review.
Cited by
- TAM-associated CASQ1 mutants diminish intracellular Ca2+ content and interfere with regulation of SOCE.
Gamberucci A, Nanni C, Pierantozzi E, Serano M, Protasi F, Rossi D, Sorrentino V. Gamberucci A, et al. J Muscle Res Cell Motil. 2024 Aug 10. doi: 10.1007/s10974-024-09681-9. Online ahead of print. J Muscle Res Cell Motil. 2024. PMID: 39126637 - The Structural-Functional Crosstalk of the Calsequestrin System: Insights and Pathological Implications.
Marabelli C, Santiago DJ, Priori SG. Marabelli C, et al. Biomolecules. 2023 Nov 23;13(12):1693. doi: 10.3390/biom13121693. Biomolecules. 2023. PMID: 38136565 Free PMC article. Review. - Structural Adaptation of the Excitation-Contraction Coupling Apparatus in Calsequestrin1-Null Mice during Postnatal Development.
Murzilli S, Serano M, Pietrangelo L, Protasi F, Paolini C. Murzilli S, et al. Biology (Basel). 2023 Jul 29;12(8):1064. doi: 10.3390/biology12081064. Biology (Basel). 2023. PMID: 37626950 Free PMC article. - Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins.
Cala SE, Carruthers NJ, Stemmer PM, Chen Z, Chen X. Cala SE, et al. Mol Cell Biochem. 2024 Jan;479(1):85-98. doi: 10.1007/s11010-023-04708-0. Epub 2023 Apr 10. Mol Cell Biochem. 2024. PMID: 37036634 Free PMC article. - Sarcoplasmic Reticulum Ca2+ Buffer Proteins: A Focus on the Yet-To-Be-Explored Role of Sarcalumenin in Skeletal Muscle Health and Disease.
Conte E, Dinoi G, Imbrici P, De Luca A, Liantonio A. Conte E, et al. Cells. 2023 Feb 24;12(5):715. doi: 10.3390/cells12050715. Cells. 2023. PMID: 36899851 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous