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...
Kaydedildi:
| Yayımlandı: | Mol Cell Biol |
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| Asıl Yazarlar: | , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Taylor & Francis
1995
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| Konular: | |
| Online Erişim: | 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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