The distinct capacity of Fyn and Lck to phosphorylate Sam68 in T cells is essentially governed by SH3/SH2-catalytic domain linker interactions

Oncogene

Volumn 21, Issue 47, 2002, Pages 7205-7213

  Feuillet, Vincent ^a   Semichon, Monique ^a   Restouin, Audrey ^b   Harriague, Julie ^a   Janzen, Julia ^c   Magee, Anthony ^c   Collette, Yves ^b   Bismuth, Georges ^a  

^a INSERM   (France)

^b INSTITUT PAOLI CALMETTES   (France)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Fyn; Lck; Sam68; Substrate specificity; T cells

Indexed keywords

GENE PRODUCT; PROTEIN KINASE FYN; PROTEIN KINASE LCK; PROTEIN SAM68; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE EXPRESSION; HUMAN; HUMAN CELL; ONCOGENE C H RAS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; T LYMPHOCYTE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; CATALYTIC DOMAIN; DNA-BINDING PROTEINS; HUMANS; JURKAT CELLS; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); PHOSPHORYLATION; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-FYN; RNA-BINDING PROTEINS; SRC HOMOLOGY DOMAINS; SUBSTRATE SPECIFICITY; T-LYMPHOCYTES;

EID: 0037126390     PISSN: 09509232     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.onc.1205929     Document Type: Article

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