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Identification of a 32K plasma membrane protein that binds to the myristylated amino-terminal sequence of p60v-src.

作者信息

Resh M D, Ling H P

机构信息

Department of Biology, Lewis Thomas Laboratory, Princeton University, New Jersey 08544.

出版信息

Nature. 1990 Jul 5;346(6279):84-6. doi: 10.1038/346084a0.

DOI:10.1038/346084a0
PMID:2164157
Abstract

The transforming protein of Rous sarcoma virus, p60v-src, is a myristylated membrane-bound phosphoprotein. Interaction of p60v-src with the plasma membrane is essential for transforming activity, and is mediated by association with a membrane-bound Src receptor protein. 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 sequences. 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 (Mr32K). 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.

摘要

相似文献

1
Identification of a 32K plasma membrane protein that binds to the myristylated amino-terminal sequence of p60v-src.
Nature. 1990 Jul 5;346(6279):84-6. doi: 10.1038/346084a0.
2
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