Key result
Human phospholamban directly binds protein phosphatase 1 regulatory subunit GM in vitro.
Why the study?
Regulation of SERCA 2a depends on the phosphorylation state of phospholamban, and the mechanism by which PP1 is targeted to PLB via GM is not fully understood.
PLB-GM interaction detected in vitro; leaves open whether GM targets PP1 to modulate cardiac SR function.
Regulation of the sarco(endo)plasmic reticulum Ca2+-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 PPI 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.
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Berrebi‐Bertrand et al. (1998) studied this question. Co-immunoprecipitation and biosensor experiments of human GM and PLB was evaluated on Biophysical interaction between human phospholamban (PLB) and protein phosphatase 1 regulatory subunit GM. In vitro experiments demonstrated a direct biophysical interaction between human phospholamban and protein phosphatase 1 regulatory subunit GM.
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