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The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes.

The catalytic activity of p56lck is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue (tyrosine 505). Accumulating data show that this phosphorylation is mediated by the tyrosine protein kinase p50csk and that it is reversed by the transmembrane tyrosine protein phosphata...

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Dades bibliogràfiques
Publicat a:Mol Cell Biol
Autors principals: Gervais, F G, Veillette, A
Format: Artigo
Idioma:Inglês
Publicat: Taylor & Francis 1995
Matèries:
Accés en línia:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC230468/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7739523/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.15.5.2393
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