Specific protein-protein interactions of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscle.
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.
Damiani
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E
Centro di Studio per la Biologia e la Fisiopatologia Muscolare, Universita' di Padova, Italy.
Margreth
A
A
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002155:Calsequestrin / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007457:Iodine Radioisotopes; D008297:Male; D009132:Muscles / Q000378:metabolism*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013045:Species Specificity; D013552:Swine
D002155:Calsequestrin; D007457:Iodine Radioisotopes; D004492:Edetic Acid; D002118:Calcium