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Titolo:
ASSOCIATION OF THE AMINO-TERMINAL HALF OF C-SRC WITH FOCAL ADHESIONS ALTERS THEIR PROPERTIES AND IS REGULATED BY PHOSPHORYLATION OF TYROSINE-527
Autore:
KAPLAN KB; BIBBINS KB; SWEDLOW JR; ARNAUD M; MORGAN DO; VARMUS HE;
Indirizzi:
UNIV CALIF SAN FRANCISCO,DEPT PHYSIOL,BOX 0444 SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT PHYSIOL SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,GRAD PROGRAM BIOPHYS SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT MICROBIOL & IMMUNOL SAN FRANCISCO CA 94143
Titolo Testata:
EMBO journal
fascicolo: 20, volume: 13, anno: 1994,
pagine: 4745 - 4756
SICI:
0261-4189(1994)13:20<4745:AOTAHO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ROUS-SARCOMA VIRUS; EXPRESS HIGH-LEVELS; SH2 DOMAIN; GENE-PRODUCT; MORPHOLOGICAL TRANSFORMATION; KINASE-ACTIVITY; PP60C-SRC; PROTEIN; BINDING; FIBROBLASTS;
Keywords:
FOCAL ADHESIONS; SH2; SH3; SRC;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
K.B. Kaplan et al., "ASSOCIATION OF THE AMINO-TERMINAL HALF OF C-SRC WITH FOCAL ADHESIONS ALTERS THEIR PROPERTIES AND IS REGULATED BY PHOSPHORYLATION OF TYROSINE-527", EMBO journal, 13(20), 1994, pp. 4745-4756

Abstract

We have characterized the mechanism by which the subcellular distribution of c-Src is controlled by the phosphorylation of tyrosine 527. Mutation of this tyrosine dramatically redistributes c-Src from endosomal membranes to focal adhesions. Redistribution to focal adhesions occurs independently of kinase activity and cellular transformation. In cells lacking the regulatory kinase (CSK) that phosphorylates tyrosine 527, c-Src is also found predominantly in focal adhesions, confirming that phosphorylation of tyrosine 527 affects the location of c-Src inside the cell. The first 251 amino acids of c-Src are sufficient to allow association with focal adhesions, indicating that at least one signal for positioning c-Src in focal adhesions resides in the amino-terminal half. Point mutations and deletions in the first 251 amino acids ofc-Src reveal that association with focal adhesions requires the myristylation site needed for membrane attachment, as well as the SH3 domain. Expression of the aminoterminal region alters both the structural and biochemical properties of focal adhesions. Focal adhesions containing this non-catalytic portion of c-Src are larger and exhibit increased levels of phosphotyrosine staining. Our results suggest that c-Src may regulate focal adhesions and cellular adhesion by a kinase-independent mechanism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 10:17:24