CLONING OF PI3 KINASE ASSOCIATED P85 UTILIZING A NOVEL METHOD FOR EXPRESSION CLONING OF TARGET PROTEINS FOR RECEPTOR TYROSINE KINASES

被引：590

作者：

SKOLNIK, EY ^{[1
]}

MARGOLIS, B ^{[1
]}

MOHAMMADI, M ^{[1
]}

LOWENSTEIN, E ^{[1
]}

FISCHER, R ^{[1
]}

DREPPS, A ^{[1
]}

ULLRICH, A ^{[1
]}

SCHLESSINGER, J ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,W-8033 MARTINSRIED,GERMANY

来源：

CELL | 1991年 / 65卷 / 01期

关键词：

D O I：

10.1016/0092-8674(91)90410-Z

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel method has been developed to allow cloning of protein targets for receptors with tyrosine kinase activity. By utilizing the carboxy-terminal tail of EGF receptor (EGFR) as a probe to screen lambda-gt11 expression libraries, several EGFR-binding proteins have been cloned; two have been analyzed and contain unique SH2 and SH3 domains. One gene (GRB-1) has been fully sequenced, is expressed in various tissues and cell lines, and has a molecular mass of 85 kd. Interestingly, GRB-1 encodes the human counterpart of the PI3 kinase-associated protein p85. Advantages of this technique include the ease of cloning tyrosine kinase receptor targets present at low levels and the ability to identify proteins that are related in their capacity to bind activated receptors but contain no significant DNA sequence homology. This method, termed CORT (for cloning of receptor targets), offers a general approach for the identification and cloning of various receptor targets.

引用

页码：83 / 90

页数：8

共 42 条

[1] BINDING OF SH2 DOMAINS OF PHOSPHOLIPASE-C-GAMMA-1, GAP, AND SRC TO ACTIVATED GROWTH-FACTOR RECEPTORS [J].