GAP相关酪氨酸磷酸化蛋白p62的分子克隆及核酸结合特性

Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62.

作者信息

Wong G, Müller O, Clark R, Conroy L, Moran M F, Polakis P, McCormick F

机构信息

Department of Molecular Biology, Chiron Corporation, Emeryville, California 94608.

出版信息

Cell. 1992 May 1;69(3):551-8. doi: 10.1016/0092-8674(92)90455-l.

DOI:10.1016/0092-8674(92)90455-l

PMID:1374686

Abstract

p62 is a tyrosine phosphoprotein that associates with p21ras GTPase-activating protein (GAP). Purification and cDNA cloning of p62 reveal extensive sequence similarity to a putative hnRNP protein, GRP33. Recombinant human p62 purified from insect Sf9 cells binds to DNA and to mRNA and, like many proteins involved in mRNA processing, recombinant p62 is modified by dimethylation on multiple arginine residues. p62 also binds tightly to p21ras GAP in vitro: this binding depends on phosphorylation of p62 on tyrosine residues and occurs through SH2 regions of GAP. These data suggest that p120-GAP and p62 play a role in some aspect of mRNA processing or utilization and that this role may be regulated by tyrosine phosphorylation, and indirectly, by p21ras.

摘要

p62是一种酪氨酸磷酸化蛋白，它与p21ras GTP酶激活蛋白（GAP）相关联。p62的纯化和cDNA克隆显示，它与一种假定的核不均一核糖核蛋白（hnRNP）——GRP33有广泛的序列相似性。从昆虫Sf9细胞中纯化得到的重组人p62能与DNA和mRNA结合，并且与许多参与mRNA加工的蛋白质一样，重组p62在多个精氨酸残基上发生二甲基化修饰。p62在体外也能与p21ras GAP紧密结合：这种结合依赖于p62酪氨酸残基的磷酸化，并且通过GAP的SH2结构域发生。这些数据表明，p120-GAP和p62在mRNA加工或利用的某些方面发挥作用，并且这种作用可能受酪氨酸磷酸化调节，并且间接受p21ras调节。