Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase.

Src family protein tyrosine kinases (PTKs) play an essential role in antigen receptor-initiated lymphocyte activation. Their activity is largely regulated by a negative regulatory tyrosine which is a substrate for the activating action of the CD45 phosphotyrosine phosphatase (PTPase) or, conversely,...

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Podrobná bibliografie
Vydáno v:	Mol Cell Biol
Hlavní autoři:	Autero, M, Saharinen, J, Pessa-Morikawa, T, Soula-Rothhut, M, Oetken, C, Gassmann, M, Bergman, M, Alitalo, K, Burn, P, Gahmberg, C G
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Taylor & Francis 1994
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC358486/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7507203/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.14.2.1308-1321.1994
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Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase.

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