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...
Gardado en:
| Publicado en: | Mol Cell Biol |
|---|---|
| Principais autores: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Taylor & Francis
1990
|
| Assuntos: | |
| Acceso en liña: | 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 |
| Tags: |
Sen Etiquetas, Sexa o primeiro en etiquetar este rexistro!
|