Phosphorylation-dependent Translocation of Glycogen Synthase to a Novel Structure during Glycogen Resynthesis

Glycogen metabolism has been the subject of extensive research, but the mechanisms by which it is regulated are still not fully understood. It is well accepted that the rate-limiting enzymes in glycogenesis and glycogenolysis are glycogen synthase (GS) and glycogen phosphorylase (GPh), respectively....

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Veröffentlicht in:	The Journal of biological chemistry 2005-06, Vol.280 (24), p.23165-23172
Hauptverfasser:	Prats, Clara, Cadefau, Joan A, Cussó, Roser, Qvortrup, Klaus, Nielsen, Jakob N, Wojtaszewski, Jørgen F P, Wojtaszewki, Jørgen F P, Hardie, D Grahame, Stewart, Greg, Hansen, Bo F, Ploug, Thorkil
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Adenosine Monophosphate - chemistry Allosteric Site Amino Acid Sequence Animals Centrifugation Cytoplasm - metabolism Cytoskeleton - metabolism Female Glycogen - chemistry Glycogen - metabolism Glycogen Phosphorylase - metabolism Glycogen Synthase - chemistry Glycogen Synthase - metabolism Image Processing, Computer-Assisted Immunohistochemistry Microscopy, Electron, Transmission Microscopy, Fluorescence Molecular Sequence Data Muscle, Skeletal - metabolism Muscle, Skeletal - ultrastructure Muscles - enzymology Muscles - metabolism Peptides - chemistry Phosphorylation Protein Conformation Protein Structure, Tertiary Protein Transport Rabbits Sarcoplasmic Reticulum - ultrastructure Subcellular Fractions - metabolism Tibia - metabolism Time Factors
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