Phosphorylation of a Novel Myosin Binding Subunit of Protein Phosphatase 1 Reveals a Conserved Mechanism in the Regulation of Actin Cytoskeleton

Journal of Biological Chemistry

Volumn 276, Issue 24, 2001, Pages 21209-21216

  Tan, Ivan ^a   Ng, Chong Han ^a   Lim, Louis ^a,b   Leung, Thomas ^a  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DEPOLYMERIZATION; PROTEINS; SUBSTRATES; TISSUE;

MOTIFS; PHOSPHORYLATION;

BIOCHEMISTRY;

ANKYRIN; BRAIN EXTRACT; LEUCINE; MESSENGER RNA; MYOSIN; MYOTONIC DYSTROPHY KINASE RELATED CDC42 BINDING KINASE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOTRANSFERASE; PROTEIN CDC42; PROTEIN P130; PROTEIN P85; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; THREONINE; UNCLASSIFIED DRUG; ACTIN; MYOTONIC DYSTROPHY PROTEIN KINASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; PROTEIN SUBUNIT; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL STRAIN COS7; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOSKELETON; DEPOLYMERIZATION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; EXPRESSED SEQUENCE TAG; HELA CELL; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; RAT; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CATALYSIS; CELL STRAIN COS1; CERCOPITHECUS; CHEMISTRY; CHROMOSOME 19; CHROMOSOME MAP; ENZYME SPECIFICITY; EXON; GENETIC TRANSFECTION; GENETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION;

ANIMALIA;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; CATALYSIS; CERCOPITHECUS AETHIOPS; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 19; CONSERVED SEQUENCE; COS CELLS; EXONS; HUMANS; MOLECULAR SEQUENCE DATA; MYOSINS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROTEIN SUBUNITS; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 0035877583     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102615200     Document Type: Article

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