期刊论文详细信息
FEBS Letters
Biophysical interaction between phospholamban and protein phosphatase 1 regulatory subunit GM
Bril, Antoine1  Souchet, Michel1  Calmels, Thierry1  Camelin, Jean-Claude1  Laville, Marie-Paule1  Berrebi-Bertrand, Isabelle1 
[1] SmithKline Beecham Laboratoires Pharmaceutiques, 4 rue du Chesnay Beauregard, P.O. Box 58, 35762 Saint-Grégoire, France
关键词: G subunit;    Protein phosphatase 1 regulatory subunit;    Phospholamban;    Interaction;    Co-immunoprecipitation;    Surface plasmon resonance;    GM;    G subunit=RG1=PPP1R3=protein phosphatase 1 (PP1) that targets the catalytic subunit (PP1C) to glycogen particles and SR;    SR;    sarcoplasmic reticulum;    SERCA;    sarco(endo)plasmic reticulum calcium ATPase;    ATPase;    adenosine triphosphatase;    DTT;    dithiothreitol;    MOPS;    3-(N-morpholino)propane sulfonic acid;    EGTA;    ethylene glycol bis-(β-aminoethyl ether) N;    N;    N′;    N′-tetraacetic acid;    SDS-PAGE;    sodium dodecyl sulphate-polyacrylamide gel electrophoresis;    PBS-T;    phosphate buffer saline-Tween 20;    Ig;    immunoglobulin;    Ig-HRP;    Ig complexed to horseradish peroxidase;    ECL;    enhanced chemiluminescence;    NHS;    N-hydroxysuccimide;    EDC;    1-ethyl-3-(3-dimethylaminopropyl) carbodiimide;    HBS;    HEPES buffer saline;    RU;    resonance unit;    GL;    targeting subunit for liver glycogen;    PTG;    for protein targeting to glycogen;    M110;    myofibrils;    PCR;    polymerase chain reaction;   
DOI  :  10.1016/S0014-5793(98)01364-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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 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.

【 授权许可】

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