Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the α4 subunit which promotes dephosphorylation of elongation factor-2

Biochemistry

Volumn 38, Issue 32, 1999, Pages 10371-10376

  Chung, Heekyoung ^a   Nairn, Angus C ^b   Murata, Kohei ^c   Brautigan, David L ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

^c OSAKA MEDICAL CENTER FOR CANCER AND CARDIOVASCULAR DISEASES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR 2; LEUCINE; PHOSPHOPROTEIN PHOSPHATASE 2A; TYROSINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DEPHOSPHORYLATION; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBUNIT; MONKEY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN METHYLATION;

ANIMALS; ANION EXCHANGE RESINS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CHROMATOGRAPHY, ION EXCHANGE; COS CELLS; HEMAGGLUTININS; LECTINS; LEUCINE; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; PEPTIDE ELONGATION FACTOR 2; PEPTIDE ELONGATION FACTORS; PEPTIDES; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEINS; PHOSPHORYLATION; PRECIPITIN TESTS; RESINS, SYNTHETIC; TRANSFECTION; TYROSINE;

EID: 0033543158     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990902g     Document Type: Article

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