IDENTIFICATION OF A 32K PLASMA-MEMBRANE PROTEIN THAT BINDS TO THE MYRISTYLATED AMINO-TERMINAL SEQUENCE OF P60V-SRC

被引:153
作者
RESH, MD
LING, HP
机构
[1] Department of Biology, Lewis Thomas Laboratory, Princeton University, Princeton
关键词
D O I
10.1038/346084a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
THE transforming protein of Rous sarcoma virus, p60v-src, is a myristylated membrane-bound phosphoprotein1-3. Interaction of p60v-src with the plasma membrane is essential for transforming activity4-5, and is mediated by association with a membrane-bound Src receptor protein6. Evidence for the existence of an Src receptor is based on the ability of a myristylated peptide containing the N-terminal Src sequence to inhibit binding of p60v-src to plasma membranes in vitro: binding of p60v-src to a plasma membrane receptor is therefore mediated by N-terminal Src sequences6. Here we report that a myristyl-Src peptide, but not the corresponding non-myristylated peptide, can be specifically crosslinked to a plasma membrane protein of relative molecular mass 32,000 (Mr 32K). The 32K protein represents an Src-binding protein in the plasma membrane that is likely to be a component of the myristyl-Src receptor, and which could be involved in cellular transformation. © 1990 Nature Publishing Group.
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页码:84 / 86
页数:3
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