Processive Phosphorylation of p130Cas by Src Depends on SH3-Polyproline Interactions

Journal of Biological Chemistry

Volumn 276, Issue 30, 2001, Pages 28190-28196

  Pellicena, Patricia ^b   Miller, W Todd ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYME KINETICS; MUTAGENESIS; SUBSTRATES; YEAST;

PHOSPHORYLATION;

ENZYMES;

CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; POLYPROPYLENE; PROTEIN TYROSINE KINASE; BCAR1 PROTEIN, HUMAN; BCAR1 PROTEIN, RAT; CRK ASSOCIATED SUBSTRATE PROTEIN; HCK PROTEIN, HUMAN; HCK PROTEIN, RAT; HEMATOPOIETIC CELL KINASE; ONCOPROTEIN; PEPTIDE; PHOSPHOPROTEIN; PHOSPHOTRANSFERASE; POLYPROLINE; PROTEIN; PROTEIN KINASE P60; PROTEIN P130; TYROSINE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL TRANSFORMATION; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME SUBSTRATE; KINETICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SRC HOMOLOGY DOMAIN; TWO HYBRID SYSTEM; YEAST; ANIMAL; BINDING SITE; CHEMISTRY; DOWN REGULATION; ENZYME ACTIVATION; GENE VECTOR; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; RAT; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; TIME;

ANIMALIA;

ANIMALS; BINDING SITES; CRK-ASSOCIATED SUBSTRATE PROTEIN; DOWN-REGULATION; ENZYME ACTIVATION; GENETIC VECTORS; HUMANS; KINETICS; MUTAGENESIS, SITE-DIRECTED; ONCOGENE PROTEIN PP60(V-SRC); PEPTIDES; PHOSPHOPROTEINS; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE KINASES; PROTEINS; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-HCK; PROTO-ONCOGENE PROTEINS PP60(C-SRC); RATS; RETINOBLASTOMA-LIKE PROTEIN P130; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; TIME FACTORS; TWO-HYBRID SYSTEM TECHNIQUES; TYROSINE;

EID: 0035958959     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M100055200     Document Type: Article

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