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Biophysical interaction between phospholamban and protein phosphatase 1 regulatory subunit GM
Author(s) -
Berrebi-Bertrand Isabelle,
Souchet Michel,
Camelin Jean-Claude,
Laville Marie-Paule,
Calmels Thierry,
Bril Antoine
Publication year - 1998
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/s0014-5793(98)01364-7
Subject(s) - phospholamban , endoplasmic reticulum , serca , protein subunit , phosphorylation , phosphatase , protein phosphatase 1 , microbiology and biotechnology , immunoprecipitation , chemistry , transmembrane protein , biology , atpase , biochemistry , gene , receptor , enzyme
Regulation of the sarco(endo)plasmic reticulum Ca 2+ ‐ATPase (SERCA 2a) depends on the phosphorylation state of phospholamban (PLB). When PLB is phosphorylated, its inhibitory effect towards SERCA 2a is relieved, leading to an enhanced myocardial performance. This process is reversed by a sarcoplasmic reticulum (SR)‐associated type 1 protein phosphatase (PP1) composed of a catalytic subunit PP1C and a regulatory subunit GM. Human GM and PLB have been produced in an in vitro transcription/translation system and used for co‐immunoprecipitation and biosensor experiments. The detected interaction between the two partners suggests that cardiac PP1 is targeted to PLB via GM and we believe that this process occurs with the identified transmembrane domains of the two proteins. Thus, the interaction between PLB and GM may represent a specific way to modulate the SR function in human cardiac muscle.