Specific protein-protein interactions of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscle

Biochemical and Biophysical Research Communications
E Damiani, A Margreth

Abstract

Minor protein components of triads and of sarcoplasmic reticulum (SR) terminal cisternae (TC), i.e. 47 and 37 kDa peptides and 31-30 kDa and 26-25 kDa peptide doublets, were identified from their ability to bind 125I calsequestrin (CS) in the presence of EGTA. The CS-binding peptides are specifically associated with the junctional membrane of TC, since they could not be detected in junctional transverse tubules and in longitudinal SR fragments. The 31-30 kDa peptide doublet, exclusively, did not bind CS in the presence of Ca2+. Thus, different types of protein-protein interactions appear to be involved in selective binding of CS to junctional TC.

References

Feb 28, 1990·Biochemical and Biophysical Research Communications·J H CollinsN Ikemoto
Feb 1, 1990·Journal of Muscle Research and Cell Motility·E DamianiA Margreth
Mar 1, 1988·The American Journal of Physiology·G Salviati, P Volpe
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Jul 1, 1987·The Journal of Cell Biology·C Franzini-ArmstrongE Varriano-Marston
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Citations

Jan 1, 1992·Progress in Biophysics and Molecular Biology·A F Dulhunty
Sep 17, 2002·European Journal of Biochemistry·Louise GloverKay Ohlendieck
Apr 3, 2012·Journal of Muscle Research and Cell Motility·Sanni Kinnunen, Satu Mänttäri
Oct 20, 2004·Molecular Pharmacology·Il Yeong ParkChulHee Kang
Aug 13, 1999·Journal of Applied Physiology·T G Favero
Jun 1, 1994·The American Journal of Physiology·R CoronadoD M Vaughan

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