Focal Adhesion Kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism

Journal of Biological Chemistry

Volumn 286, Issue 19, 2011, Pages 17292-17302

  Plaza Menacho, Iván ^a,f   Morandi, Andrea ^a   Mologni, Luca ^b   Boender, Piet ^c   Gambacorti Passerini, Carlo ^b   Magee, Anthony I ^d   Hofstra, Robert M W ^e   Knowles, Phillip ^f   McDonald, Neil Q ^f   Isacke, Clare M ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^b UNIVERSITY OF MILANO BICOCCA   (Italy)

^c PamGene International BV   (Netherlands)

^d NATIONAL HEART AND LUNG INSTITUTE   (United Kingdom)

^e UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

^f IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL-BASED; DOWN-REGULATION; DOWNSTREAM TARGET; FOCAL ADHESION KINASE; IN-VITRO; KINASE DOMAINS; KINASE INHIBITORS; OLIGOPEPTIDES; PEPTIDE ARRAYS; PHOSPHOTYROSINE BINDING DOMAINS; SMALL MOLECULE INHIBITOR; SRC HOMOLOGY 2; THERAPEUTIC AGENTS; TRANSACTIVATION; TRANSFECTED CELLS; WILD TYPES;

ADHESION; CELL CULTURE; ENZYME KINETICS; PATIENT TREATMENT; SIGNALING; SUBSTRATES; TUMORS;

PHOSPHORYLATION;

FOCAL ADHESION KINASE; PROTEIN RET;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; HUMAN; HUMAN CELL; IN VITRO STUDY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; TRANSACTIVATION; WILD TYPE;

ANTINEOPLASTIC AGENTS; CELL PROLIFERATION; FOCAL ADHESION PROTEIN-TYROSINE KINASES; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; OLIGOPEPTIDES; PHENOTYPE; PHOSPHORYLATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-RET; SIGNAL TRANSDUCTION; TRANSCRIPTIONAL ACTIVATION;

EID: 79955783528     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.168500     Document Type: Article

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