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Titolo:
c-Cbl localizes to actin lamellae and regulates lamellipodia formation andcell morphology
Autore:
Scaife, RM; Langdon, WY;
Indirizzi:
Univ Western Australia, Dept Pathol, QE II Med Ctr, Nedlands, WA 6907, Australia Univ Western Australia Nedlands WA Australia 6907 nds, WA 6907, Australia
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 2, volume: 113, anno: 2000,
pagine: 215 - 226
SICI:
0021-9533(200001)113:2<215:CLTALA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOTYROSINE-BINDING DOMAIN; INTEGRIN SIGNALING PATHWAY; T-CELLS; V-CBL; TYROSINE PHOSPHORYLATION; NEGATIVE REGULATOR; FOCAL ADHESIONS; STRESS FIBERS; EGF RECEPTOR; PRODUCT;
Keywords:
Cbl; actin cytoskeleton; src-homology; signal transduction; cell shape;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Scaife, RM Univ Western Australia, Dept Pathol, QE II Med Ctr, Nedlands, WA 6907, Australia Univ Western Australia Nedlands WA Australia 6907 7, Australia
Citazione:
R.M. Scaife e W.Y. Langdon, "c-Cbl localizes to actin lamellae and regulates lamellipodia formation andcell morphology", J CELL SCI, 113(2), 2000, pp. 215-226

Abstract

Adhesive and locomotive properties of cells have key roles in normal phlysiology and disease, Cell motility and adhesion require the assembly and organization of actin microfilaments into stress fibers, lamellipodia and filopodia, and the formation of these structures is mediated by signalling through Rho GTPases, Here we identify c-Cbl (a multi-adaptor proto-oncogene product involved in protein tyrosine kinase signalling) as an important regulator of the actin cytoskeleton, By immunofluorescence microscopy we have determined that c-Cbl co-localizes with the adaptor protein Crk to submembranous actin lamellae in NIH 3T3 fibroblasts and that c-Cbl's actin localization requires specific SH3-binding sequences, Further, we have found that truncation of this SH3-binding domain in c-Cbl profoundly alters the morphologyof NIH 3T3 fibroblasts by inhibiting the formation of actin lamellae, lamellipodia and membrane ruffles. The induction of lamellipodia and membrane ruffles are also inhibited during cell spreading and migration, conditions when these structures are normally most prominent. The inhibitory effect of truncated c-Cbl expression on lamellipodia formation can be reversed by mutational inactivation of its divergent SH2 domain, by expression of constitutively active Rac or by the overexpression of c-Cbl, This study therefore identifies a cytoskeletal role for c-Cbl which may involve the regulation ofCrk and Rac, and which is dependent on targeting of c-Cbl to actin lamellae and the ability to recruit signalling protein(s) associated with its divergent SH2 domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 05:26:43