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Titolo:
SRC-INDUCED ACTIVATION OF INDUCIBLE T-CELL KINASE (ITK) REQUIRES PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY AND THE PLECKSTRIN HOMOLOGY DOMAIN OF INDUCIBLE T-CELL KINASE
Autore:
AUGUST A; SADRA A; DUPONT B; HANAFUSA H;
Indirizzi:
ROCKEFELLER UNIV,MOL ONCOL LAB,1230 YORK AVE NEW YORK NY 10021 ROCKEFELLER UNIV,MOL ONCOL LAB NEW YORK NY 10021 MEM SLOAN KETTERING CANC CTR,PROGRAM IMMUNOL NEW YORK NY 10021
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 21, volume: 94, anno: 1997,
pagine: 11227 - 11232
SICI:
0027-8424(1997)94:21<11227:SAOITK>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
BRUTONS TYROSINE KINASE; X-LINKED AGAMMAGLOBULINEMIA; RI CROSS-LINKING; FAMILY KINASE; HEMATOPOIETIC-CELLS; PROTEIN; GENE; EXPRESSION; BINDING; CD28;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
A. August et al., "SRC-INDUCED ACTIVATION OF INDUCIBLE T-CELL KINASE (ITK) REQUIRES PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY AND THE PLECKSTRIN HOMOLOGY DOMAIN OF INDUCIBLE T-CELL KINASE", Proceedings of the National Academy of Sciences of the United Statesof America, 94(21), 1997, pp. 11227-11232

Abstract

The Tec family of tyrosine kinases are involved in signals emanating from cytokine receptors, antigen receptors, and other lymphoid cell surface receptors. One family member, ITK (inducible T cell kinase), is involved in T cell activation and can be activated by the T cell receptor and the CD28 cell surface receptor. This stimulation of tyrosine phosphorylation and activation of ITK can be mimicked by the Src familykinase Lck We have explored the mechanism of this requirement for Srcfamily kinases in the activation of ITK, We found that coexpression of ITK and Src results in increased membrane association, tyrosine phosphorylation and activation of ITK, which could be blocked by inhibitors of the lipid kinase phosphatidylinositol 3-kinase (PI 3-kinase) as well as overexpression of the p85 subunit of PI 3-kinase. Removal of the Pleckstrin homology domain (PH) of ITK resulted in a kinase that could no longer be induced to localize to the membrane or be activated bySrc. The PH of ITK was also able to bind inositol phosphates phosphorylated at the D3 position. Membrane targeting of ITK without the PH recovered its ability to be activated by Src, These results suggest thatITK can be activated by a combination of Src and PI 3-kinase.

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Documento generato il 08/04/20 alle ore 09:13:55