Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.
Mutation of the major site of in vivo tyrosine phosphorylation of p56lck (tyrosine 505) to a phenylalanine constitutively enhances the p56lck-associated tyrosine-specific protein kinase activity. The mutant polypeptide is extensively phosphorylated in vivo at the site of in vitro Lck autophosphoryla...
שמור ב:
| הוצא לאור ב: | Mol Cell Biol |
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| Principais autores: | , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
Taylor & Francis
1990
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC361199/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1697929/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.10.10.5197-5206.1990 |
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