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
Celljournal_title
Cellauthors
Resh MDdoi
10.1016/0092-8674(89)90842-8subject
Has Abstractpub_date
1989-07-28 00:00:00pages
281-6issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(89)90842-8journal_volume
58pub_type
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