过表达的pp60c-src中自磷酸化位点的调控
Regulation by the autophosphorylation site in overexpressed pp60c-src.
作者信息
Kmiecik T E, Johnson P J, Shalloway D
机构信息
Department of Molecular and Cell Biology, Pennsylvania State University, University Park, 16802.
出版信息
Mol Cell Biol. 1988 Oct;8(10):4541-6. doi: 10.1128/mcb.8.10.4541-4546.1988.
Abstract
We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.
摘要
我们发现，过表达的pp60c-src在酪氨酸416位点发生磷酸化，并且当从与酪氨酸磷酸酶抑制剂钒酸盐孵育的细胞中分离出来时，其比激酶活性增加。这支持了这样一种假说，即酪氨酸416位点的瞬时磷酸化在体内调节过表达的pp60c-src的活性。诱变表明，酪氨酸416位点也调节pp60v-src的活性。
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