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Titolo:
MUTAGENIC ANALYSIS OF VAV REVEALS THAT AN INTACT SH3 DOMAIN IS REQUIRED FOR TRANSFORMATION
Autore:
GROYSMAN M; NAGANO M; SHAANAN B; KATZAV S;
Indirizzi:
HEBREW UNIV JERUSALEM,HADASSAH MED SCH,HUBERT H HUMPHREY CTR EXPT MED& CANC RES IL-91120 JERUSALEM ISRAEL HEBREW UNIV JERUSALEM,HADASSAH MED SCH,HUBERT H HUMPHREY CTR EXPT MED& CANC RES IL-91120 JERUSALEM ISRAEL HEBREW UNIV JERUSALEM,INST LIFE SCI,DEPT BIOL CHEM IL-91904 JERUSALEMISRAEL
Titolo Testata:
Oncogene
fascicolo: 12, volume: 17, anno: 1998,
pagine: 1597 - 1606
SICI:
0950-9232(1998)17:12<1597:MAOVRT>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SUBSTITUTIONS; TYROSINE KINASE-ACTIVITY; PROLINE-RICH PEPTIDES; GTP EXCHANGE FACTOR; PROTOONCOGENE PRODUCT; C-SRC; SIGNAL-TRANSDUCTION; T-CELL; BINDING-PROTEIN; GENE;
Keywords:
VAV; SH3; ZYXIN; HNRNP-K;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
M. Groysman et al., "MUTAGENIC ANALYSIS OF VAV REVEALS THAT AN INTACT SH3 DOMAIN IS REQUIRED FOR TRANSFORMATION", Oncogene, 17(12), 1998, pp. 1597-1606

Abstract

The vav proto-oncogene encodes a protein with multiple modulae domains that enable it to function as a mediator, linking tyrosine signalingto downstream events in hematopoietic cells, Circumstantial evidence suggests that protein-protein interactions exerted by two of these domains, the Src homology 2 (SH2) and the Src homology 3 (SH3), play an important role in the regulation of Vav activity, To study the relevance of the SH3 domain for the function of vav as a transforming gene, wehave created several mutations in the SH3 domain located at its carboxy region. Substitution of the non-conserved aspartic acid 797 (to asparagine, D797N) retained the transforming potential of the vav oncogene, whereas substitutions of five highly conserved amino-acids: alanine789 (to asparagine, A789N), leucine 801 (to arginine, L801R), tryptophan 821 (to arginine, W821R), glycine 830 (to valine, G830V) and valine 837 (to glutamic acid, V837E) greatly reduced its transforming potential. The mutant proteins resemble Vav in many biochemical properties;however, while the transforming mutant protein (D797N) associates with several unidentified proteins in a manner similar to that of Vav, the non-transforming mutant Vav proteins react very poorly with these proteins, Among the known Vav-interacting proteins, hnRNP-K associates with all mutant proteins except A789N and V837E whereas binding of Zyxin to any of the mutant proteins is not affected. Taken together, our results clearly demonstrate that the SH3 domain has a positive effect on vav activity and is needed for vav transformation, The vavSH3C associating protein(s) that are crucial for its activity as a transforming gene have probably not Set been identified.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 17:41:36