pp60c-src variants containing lesions that affect phosphorylation at tyrosines 416 and 527.
نویسندگان
چکیده
منابع مشابه
Phosphorylation of tyrosine in the carboxyl-terminal tryptic peptide of pp60c-src.
The major site of tyrosine phosphorylation of the transforming protein of Rous sarcoma virus, pp60v-src (tyrosine-416), is different from the major site of tyrosine phosphorylation of its nontransforming normal cellular counterpart, pp60c-src. We have shown that antibodies against a synthetic peptide modeled on the carboxyl-terminal 13 residues of pp60c-src specifically immunoprecipitate the ma...
متن کاملIn vivo effect of sodium orthovanadate on pp60c-src kinase.
We have compared the tyrosine kinase activity of pp60c-src isolated from intact chicken embryo fibroblasts treated with micromolar sodium orthovanadate for 4 h and from untreated cells. We found an approximate 50% reduction in both autophosphorylation of pp60c-src and phosphorylation of casein when examined in the immune complex kinase assay. The reduction of in vitro enzymatic activity correla...
متن کاملRole of p34cdc2-mediated phosphorylations in two-step activation of pp60c-src during mitosis.
Phosphorylation of pp60c-src by p34cdc2 at three amino-proximal serine/threonine residues is temporally correlated with, but insufficient for, mitotic activation of c-Src kinase. The direct cause of activation during mitosis appears to be temporally correlated partial dephosphorylation of Tyr-527, a residue whose phosphorylation strongly suppresses pp60c-src activity. Site-directed mutagenesis ...
متن کاملPurification and biochemical characterization of non-myristoylated recombinant pp60c-src kinase.
To obtain sufficient material for the biochemical and biophysical study of pp60c-src, we have utilized a recombinant pp60c-src baculovirus lacking the myristoylation site at codon 2. On infection of Sf9 cells, this virus produced large amounts of soluble non-myristoylated pp60c-src. The use of non-myristoylated pp60c-src (1) increases production of pp60c-src compared with the wild-type protein,...
متن کاملHigh pp60c-src level in human platelet dense bodies.
Phosphoproteins phosphorylated in vivo were examined in resting and thrombin-activated human blood platelets. Thrombin-stimulation resulted in an overall increase in labeled proteins containing phosphotyrosine. The most prominent was a protein of 60 Kd. By electroblotting, the 60 Kd protein was identified as the pp60c-src, the normal cellular homolog of the transforming protein of Rous sarcoma ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1989
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.9.9.3647