P62 ASSOCIATION WITH RNA IS REGULATED BY TYROSINE PHOSPHORYLATION
P62 ASSOCIATION WITH RNA IS REGULATED BY TYROSINE PHOSPHORYLATION
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DOI：
10.1074/jbc.270.5.2010
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发表时间：
1995-02-03
影响因子：
4.8
通讯作者：
SHAW, AS
中科院分区：
文献类型：
--
作者：
WANG, LL;RICHARD, S;SHAW, AS
ras-GAP 相关蛋白 p62 是转化和生长因子处理细胞中的主要酪氨酸磷蛋白，虽然其确切功能尚不清楚，但它可以直接与 src 家族酪氨酸激酶结合，并且被认为是桥接激活的 src 家族酪氨酸激酶与下游效应子的连接蛋白。通过其预测的氨基酸序列揭示的 p62 的一个新特征是存在 RNA 结合区域，即 KH 结构域。由于当src激酶被激活时p62变得酪氨酸磷酸化，我们比较了p62在磷酸化和非磷酸化状态下的RNA结合能力。当p62被酪氨酸磷酸化时，p62结合RNA的能力被严重削弱。这表明 p62 结合 RNA 的能力受到酪氨酸磷酸化的调节，并暗示 RNA 作为酪氨酸激酶信号通路的一个组成部分的调节。
The ras-GAP associated protein, p62, is a major tyrosine phosphoprotein in transformed and growth factor treated cells, Although its exact function is not known, it can bind directly to src-family tyrosine kinases and has been implicated as a linker protein bridging activated src family tyrosine kinases with downstream effecters, One novel feature of p62, revealed by its predicted amino acid sequence, is the presence of an RNA-binding region, the KH domain. As p62 becomes tyrosine phosphorylated when src-kinases become activated, we compared the RNA binding ability of p62 in both its phosphorylated and unphosphorylated state, The ability of p62 to bind RNA was severely impaired when p62 was tyrosine phosphorylated. This suggests that the ability of p62 to bind RNA is regulated by tyrosine phosphorylation and implicates the regulation of RNA as a component of tyrosine kinase signaling pathways.