Specific and saturable binding of pp60v-src to plasma membranes: evidence for a myristyl-src receptor.

Abstract:

:The molecular basis for membrane association of pp60v-src, the transforming protein of Rous sarcoma virus, was investigated in a cell-free system. Newly synthesized pp60v-src polypeptide, produced by in vitro translation of src mRNA, rapidly bound to plasma membranes. Binding was saturable and dependent on the presence of myristate at the amino terminus of pp60v-src. Prior treatment of membranes with heat or trypsin greatly decreased subsequent binding of pp60v-src. Membrane binding of pp60v-src was competed by a myristylated peptide containing the first 11 amino acids of the mature src sequence, but not by non-myristylated src peptide or other myristylated peptides. The specificity, saturability, and competitive nature of pp60v-src binding provide evidence for the existence of a src receptor in the plasma membrane.

journal_name

Cell

journal_title

Cell

authors

Resh MD

doi

10.1016/0092-8674(89)90842-8

subject

Has Abstract

pub_date

1989-07-28 00:00:00

pages

281-6

issue

2

eissn

0092-8674

issn

1097-4172

pii

0092-8674(89)90842-8

journal_volume

58

pub_type

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