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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| Gepubliceerd in: | Mol Cell Biol |
|---|---|
| Hoofdauteurs: | , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Taylor & Francis
1995
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| Onderwerpen: | |
| Online toegang: | 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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