Does phosphorylase kinase control glycogen biosynthesis in skeletal muscle?

FEBS Letters

Heilmeyer, Ludwig M.G.²  Varsányi, Magdolna²  Meyer, Helmut E.²  Polishchuk, Sergey V.²  Brandt, Neil R.¹ 

[1] Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, FL 33101, USA;Abteilung für Biochemie Supramolekularer Systeme, Institut für Physiologische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany

关键词: Glycogen biosynthesis;    Glycogenin;    Proglycogen;    Skeletal muscle;    Phosphorylase kinase;    SR;    sarcoplasmic reticulum;    HSR;    heavy SR vesicles;    PVDF;    polyvinylidene difluoride;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel-electrophoresis;   

DOI  :  10.1016/0014-5793(95)00260-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Immunoblotting as well as enzyme assays demonstrate the presence of the self-glucosylating protein, glycogenin, in the protein-glycogen complex, in the sarcoplasmic reticulum and in phosphorylase kinase. In all three compartments glycogenin occurs in different, albeit, defined glucosylated forms, which upon deglucosylation are converted into a 42 kDa form. We suggest that phosphorylase kinase might have a dual function in glycogen biogenesis: firstly, control of glycogen degradation in the protein-glycogen complex via phosphorylation of glycogen phosphorylase b; secondly, regulation of glycogen biosynthesis on the sarcoplasmic reticular membranes via phosphorylation and thereby inhibition of glycogen synthase.

【 授权许可】

Unknown