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Titolo:
The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes
Autore:
Summy, JM; Guappone, AC; Sudol, M; Flynn, DC;
Indirizzi:
W Virginia Univ, Mary Babb Randolph Canc Ctr, Morgantown, WV 26506 USA W Virginia Univ Morgantown WV USA 26506 anc Ctr, Morgantown, WV 26506 USA W Virginia Univ, Dept Microbiol & Immunol, Morgantown, WV 26506 USA W Virginia Univ Morgantown WV USA 26506 Immunol, Morgantown, WV 26506 USA CUNY Mt Sinai Sch Med, Dept Biochem, New York, NY 10029 USA CUNY Mt Sinai Sch Med New York NY USA 10029 ochem, New York, NY 10029 USA
Titolo Testata:
ONCOGENE
fascicolo: 1, volume: 19, anno: 2000,
pagine: 155 - 160
SICI:
0950-9232(20000106)19:1<155:TSASDA>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-COLON-CARCINOMA; SRC FAMILY KINASES; C-SRC; BINDING-SPECIFICITY; COMPLEX-FORMATION; GENE-PRODUCT; YES; ASSOCIATION; ACTIVATION; CELLS;
Keywords:
Src; Yes; SH3; SH2; tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Flynn, DC W Virginia Univ, Mary Babb Randolph Canc Ctr, POB 9300, Morgantown, WV 26506 USA W Virginia Univ POB 9300 Morgantown WV USA 26506 n, WV 26506 USA
Citazione:
J.M. Summy et al., "The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes", ONCOGENE, 19(1), 2000, pp. 155-160

Abstract

The c-src and eyes proto-oncogenes encode 60 000 and 62 000 Dalton non-receptor tyrosine kinases of the Src family, pp60(c-src) and pp62(c-yes), respectively. These kinases are over 80% homologous outside of their unique amino termini, yet several studies suggest that differences exist in the regulation, activation, and function of cSrc and c Yes. The determinants of specificity in signaling between these proteins, however, remain unclear, In order to investigate the roles of the Src Homology (SH) 3 and 2 domains in mediating signaling specificity between cSrc and cYes, chimeras were created in which the SH3 and/or SH2 domains of cSrc or the fully activated variant Src(527F) were replaced by the corresponding domains of cYes. These constructs were used to assess the effects of the Yes SH3 and SH2 domains on the ability of Src to form stable complexes with and induce tyrosine phosphorylation of Src SH3 and SH2 domain binding partners in vivo. Both the Yes SH3 and SH2 domains were found to alter the capacity of Src to form stable associations with heterologous proteins. The Yes SH3 domain was unable to affinity absorb the Src SN3/SH2 binding partner AFAP-110 from COS-1 cell lysates,and chimeric constructs of Src(527F) containing the cYes SH3 domain were unable to efficiently coimmunoprecipitate with AFAP-110 from chicken embryo fibroblasts. Interactions with the Src SH2 domain binding partner pp130cas were unaffected, Additionally only chimeras containing the cYes SH2 domain were able to co-immunoprecipitate with an unidentified 87 kDa tyrosine-phosphorylated protein. These results indicate that the SH3 and SH2 domains arecapable of directing specificity in substrate binding between Src and Yes,suggesting potential mechanisms for generating specificity in signaling between these two highly related non-receptor tyrosine kinases.

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Documento generato il 03/12/20 alle ore 12:25:07