Inhibition of protein phosphorylation modulates expression of the Jak family protein tyrosine kinases.
AUTOR(ES)
Fiorucci, G
RESUMO
Treatment of murine Friend cells with a dose of the protein kinase inhibitor staurosporine, which is able to block the response of the cells to interferons, appears to inhibit phosphorylation of Jak proteins and, interestingly, to specifically reduce tyk2 and Jak1 expression and to increase Jak2 both in the presence and in the absence of interferons. Therefore, a potential role for phosphorylation events in the regulation of expression of the Jak family members is suggested.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=189453Documentos Relacionados
- Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases.
- Regulation of Btk by Src family tyrosine kinases.
- Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases.
- Differential modulation of plasminogen activator gene expression by oncogene-encoded protein tyrosine kinases.
- Association between B-lymphocyte membrane immunoglobulin and multiple members of the Src family of protein tyrosine kinases.
