p66shc inhibits insulin-like growth factor-I signaling via direct binding to Src through its polyproline and Src homology 2 domains, resulting in impairment of Src kinase activation

Journal of Biological Chemistry

Volumn 285, Issue 10, 2010, Pages 6937-6951

  Xi, Gang ^a   Shen, Xinchun ^a   Clemmons, David R ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL STRESS; GROWTH FACTOR; IN-VITRO; INSULIN-LIKE GROWTH FACTOR-I; POLYPROLINE; PROLINE RESIDUES; SEQUENCE MOTIFS; SRC HOMOLOGY 2 DOMAINS; SRC-KINASE; SYNTHETIC PEPTIDE;

BIOACTIVITY; CELL PROLIFERATION; CHEMICAL ACTIVATION; PHOSPHORYLATION;

PEPTIDES;

GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; POLYPROLINE; PROLINE; PROTEIN P52; PROTEIN P52 SHC; PROTEIN P66; PROTEIN P66 SHC; PROTEIN SH2; PROTEIN SHC; PROTEIN TYROSINE KINASE; SOMATOMEDIN C; UNCLASSIFIED DRUG; DIFFERENTIATION ANTIGEN; IMMUNOGLOBULIN RECEPTOR; MULTIPROTEIN COMPLEX; PEPTIDE; PHOSPHOTYROSINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL PROLIFERATION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME BINDING; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; GENE DELETION; GENE OVEREXPRESSION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; ANIMAL; AORTA; CELL CULTURE; CYTOLOGY; DRUG ANTAGONISM; GENETICS; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; SMOOTH MUSCLE FIBER; SRC HOMOLOGY DOMAIN; SWINE;

ANIMALS; ANTIGENS, DIFFERENTIATION; AORTA; CELLS, CULTURED; ENZYME ACTIVATION; GRB2 ADAPTOR PROTEIN; HUMANS; INSULIN-LIKE GROWTH FACTOR I; MITOGEN-ACTIVATED PROTEIN KINASES; MULTIPROTEIN COMPLEXES; MYOCYTES, SMOOTH MUSCLE; PEPTIDES; PHOSPHOTYROSINE; PROTEIN BINDING; RECEPTORS, IMMUNOLOGIC; SHC SIGNALING ADAPTOR PROTEINS; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; SWINE;

EID: 77951246552     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.069872     Document Type: Article

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