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Titolo:
The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction
Autore:
Kirsch, KH; Georgescu, MM; Shishido, T; Langdon, WY; Birge, RB; Hanafusa, H;
Indirizzi:
Rockefeller Univ, Mol Oncol Lab, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 Oncol Lab, New York, NY 10021 USA Rockefeller Univ, Lab Mol Genet & Immunol, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 & Immunol, New York, NY 10021 USA Univ Western Australia, Dept Pathol, Nedlands, WA 6907, Australia Univ Western Australia Nedlands WA Australia 6907 nds, WA 6907, Australia Osaka Biosci Inst, Suita, Osaka 5650874, Japan Osaka Biosci Inst Suita Osaka Japan 5650874 , Suita, Osaka 5650874, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 7, volume: 276, anno: 2001,
pagine: 4957 - 4963
SICI:
0021-9258(20010216)276:7<4957:TATPCB>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEDIATED NEGATIVE REGULATION; GROWTH-FACTOR RECEPTOR; CELL ANTIGEN RECEPTOR; EGF RECEPTOR; PHOSPHATIDYLINOSITOL 3-KINASE; SIGNAL-TRANSDUCTION; IN-VIVO; PROTOONCOGENE PRODUCT; SH3 DOMAINS; T-CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Kirsch, KH Rockefeller Univ, Mol Oncol Lab, Box 220, New York, NY 10021 USA Rockefeller Univ Box 220 New York NY USA 10021 rk, NY 10021 USA
Citazione:
K.H. Kirsch et al., "The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction", J BIOL CHEM, 276(7), 2001, pp. 4957-4963

Abstract

CMS/CD2AP is a cytoplasmic protein critical for the integrity of the kidney glomerular filtration and the T cell function. CMS contains domains and motifs characteristic for protein-protein interactions, and it is involved in the regulation of the actin cytoskeleton, We report here that the individual SH3 domains of CMS bind to phosphotyrosine proteins of similar to 80, 90, and 180 kDa in cell lysates stimulated with epidermal growth factor. Thesecond SH3 domain of CMS bound specifically to a tyrosine-phosphorylated protein of 120 kDa, which we identified as the proto-oncoprotein c-Cbl. The c-Cbl-binding site for CMS mapped to the carboxyl terminus of c-Cbl and is different from the proline-rich region known to bind SH3-containing proteins. CMS binding to c-Cbl was markedly attenuated in a tyrosine phosphorylation-defective c-Cbl mutant indicating that this interaction is dependent on the tyrosine phosphorylation of CMS. It also implies that CMS interacts with c-Cbl in an inducible fashion upon stimulation of a variety of cell-surface receptors. Immunofluorescence analysis revealed that both proteins colocalize at lamellipodia and leading edges of cells, and we propose that the interaction of CMS with c-Cbl offers a mechanism by which c-Cbl associates and regulates the actin cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 11:45:55