PTG, a protein phosphate 1-binding protein with a role in glycogen metabolism

Science

Volumn 275, Issue 5305, 1997, Pages 1475-1478

  Printen, John A ^a,b   Brady, Matthew J ^b   Saltiel, Alan R ^a,b  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GLYCOGEN; INSULIN RECEPTOR; PHOSPHOPROTEIN PHOSPHATASE; CARRIER PROTEIN; COMPLEMENTARY DNA; GLYCOGEN PHOSPHORYLASE; GLYCOGEN SYNTHASE; HYBRID PROTEIN; INSULIN; PHOSPHORYLASE KINASE; PPP1R3C PROTEIN, MOUSE; SIGNAL PEPTIDE;

ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CHO CELL; CONTROLLED STUDY; GLYCOGEN METABOLISM; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; TISSUE DISTRIBUTION; AMINO ACID SEQUENCE; ANIMAL; BIOSYNTHESIS; CHEMISTRY; ENZYME SPECIFICITY; GENETIC TRANSFECTION; GENETICS; HAMSTER; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN BINDING;

3T3 CELLS; AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; DNA, COMPLEMENTARY; GLYCOGEN; GLYCOGEN SYNTHASE; INSULIN; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MICE; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLASE A; PHOSPHORYLASE KINASE; PHOSPHORYLATION; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 0030614364     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5305.1475     Document Type: Article

References (36)

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26. CHO-IR cells were washed three times with ice-cold phosphate-buffered saline, scraped in homogenization buffer, and samples sonicated and centrifuged at 2500g to remove nuclei and unlysed cells. The postnuclear supernatant was removed and centrifuged for 15 min at 10,000g and 1 hour at 100,00Og to pellet plasma membranes and glycogen pellets, respectively. The final supernatant was called cytosol.
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36. We thank M. Chang for the pCl-neo/FLAG construct, A. Nairn for PP1α cDNA, and J. Lawrence for antibodies to PP1Cα and glycogen synthase.