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Titolo:
INTERACTIONS OF THE SH2 DOMAIN OF LYMPHOCYTE-SPECIFIC TYROSINE PROTEIN-KINASE P56(LCK) WITH PHOSPHOTYROSINE-CONTAINING PROTEINS
Autore:
PERI KG; GERVAIS FG; WEIL R; DAVIDSON D; GISH GD; VEILLETTE A;
Indirizzi:
MCGILL UNIV,MCGILL CANC CTR,ROOM 715B,MCINTYRE MED SCI BLDG,3655 DRUMMOND ST MONTREAL H3G 1Y6 QUEBEC CANADA MCGILL UNIV,MCGILL CANC CTR,ROOM 715B,MCINTYRE MED SCI BLDG,3655 DRUMMOND ST MONTREAL H3G 1Y6 QUEBEC CANADA MCGILL UNIV,DEPT BIOCHEM MONTREAL H3G 1Y6 QUEBEC CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST TORONTO M5G 1X5 ONTARIO CANADA MCGILL UNIV,DEPT MED MONTREAL H3G 1Y6 QUEBEC CANADA MCGILL UNIV,DEPT ONCOL MONTREAL H3G 1Y6 QUEBEC CANADA MONTREAL GEN HOSP,DEPT MED,DIV MED ONCOL MONTREAL H3G 1A4 QUEBEC CANADA
Titolo Testata:
Oncogene
fascicolo: 10, volume: 8, anno: 1993,
pagine: 2765 - 2772
SICI:
0950-9232(1993)8:10<2765:IOTSDO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ANTIGEN RECEPTOR; PHOSPHOLIPASE C-GAMMA-1; SIGNAL TRANSDUCTION; CATALYTIC ACTIVITY; P56LCK; SRC; PHOSPHORYLATION; LCK; RESPONSIVENESS; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
K.G. Peri et al., "INTERACTIONS OF THE SH2 DOMAIN OF LYMPHOCYTE-SPECIFIC TYROSINE PROTEIN-KINASE P56(LCK) WITH PHOSPHOTYROSINE-CONTAINING PROTEINS", Oncogene, 8(10), 1993, pp. 2765-2772

Abstract

We have previously demonstrated that the non-catalytic Src homology 2(SH2) domain is required for both positive and negative regulation ofthe catalytic function of the lymphocyte-specific tyrosine protein kinase p56lck. Indeed, the ability of activated p56lck molecules (tyrosine 505 to phenylalanine 505 mutants) to enhance T-cell receptor (TCR)-induced tyrosine protein phosphorylation is dramatically reduced by deletion of the SH2 domain. Paradoxically, removal of the SH2 sequence also results in constitutive elevation of the catalytic function of wild-type Lck polypeptides, rendering them capable of oncogenic transformation of rodent fibroblasts. As SH2 sequences can mediate binding to phosphotyrosine-containing peptides, the ability of the Lck SH2 domain to interact with tyrosine-phosphorylated proteins was tested. We foundthat the SH2 sequence of p56lck can bind several of the TCR-regulatedtyrosine phosphorylation substrates in vitro. One of the substrates, an 80-kilodalton (kDa) phosphoprotein (p80) showed the tightest binding to the SH2 domain of Lck. Additionally, it was observed that the SH2domain of Lck can bind a synthetic peptide containing the phosphorylated carboxy-terminal tyrosine 505 of p56lck. Indirect evidence indicating that the SH2 region interacts with the tyrosine-phosphorylated carboxy terminus of Lck in vivo was also obtained. As deletion of the SH2domain or mutation of tyrosine 505 results in p56lck activation in vivo, it is conceivable that interactions between these two regions impose a conformation that is unfavorable to phosphorylation of intracellular substrates. Collectively, these findings suggest that the SH2 domain modulates the catalytic function of Lck through complex interactions with phosphotyrosine-containing proteins.

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Documento generato il 27/11/20 alle ore 13:48:26