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Phospholamban of cardiac sarcoplasmic reticulum consists of two functionally distinct proteolipids
Author(s) -
Chiesi Michele,
Gasser Jürg,
Carafoli Ernesto
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80936-3
Subject(s) - phospholamban , endoplasmic reticulum , calmodulin , phosphorylation , protein kinase a , trypsinization , biochemistry , chemistry , microbiology and biotechnology , biology , biophysics , enzyme , trypsin
Phosphorylation of phospholamban by either a cAMP‐dependent or a calmodulin‐dependent kinase stimulates the Ca 2+ transporting activity of cardiac sarcoplasmic reticulum membranes. It has now been found that phospholamban consists of 2 distinct proteins; one is the specific substrate for the cAMP‐dependent phosphorylation, and the other for the calmodulin‐dependent kinase. In spite of functional diversity, the 2 polypeptides share a number of properties. Among them, the proteolipid character, M r , resistance to trypsinization, and subunit composition.