Phosphoserine as a recognition determinant for glycogen synthase kinase-3: Phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1

Archives of Biochemistry and Biophysics

Volumn 267, Issue 2, 1988, Pages 797-802

  Fiol, Carol J ^a   Haseman, Joseph H ^a   Wang, Yuhuan ^a   Roach, Peter J ^a   Roeske, Roger W ^a   Kowalczuk, Maria ^a   DePaoli Roach, Anna A ^a  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOSERINE; RADIOISOTOPE;

ENZYME PHOSPHORYLATION; GLYCOGEN SYNTHASE KINASE 3; MOLECULAR RECOGNITION; PRIORITY JOURNAL;

ARGININE; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; GLYCOGEN-SYNTHASE-D PHOSPHATASE; ISOELECTRIC FOCUSING; PEPTIDES; PHOSPHATES; PHOSPHOPEPTIDES; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PHOSPHOSERINE; PROTEIN KINASES; SERINE; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TRYPSIN;

EID: 0024233098     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/0003-9861(88)90089-6     Document Type: Article

References (14)

1. Protein Phosphorylation Catalyzed by Cyclic AMP-Dependent and Cyclic GMP-Dependent Protein Kinases
2. The protein phosphatases involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle
3. Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G by cyclic-AMP-dependent protein kinase promotes translocation of the phosphatase from glycogen to cytosol in rabbit skeletal muscle