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Binding of pp60v-src to membranes: evidence for multiple membrane interactions
L Silverman1, C T Sigal, M D Resh
1Department of Cell Biology and Genetics, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|October 1, 1992
Summary
Myristylated Rous sarcoma virus protein pp60v-src membrane association is receptor-mediated. Internal domains influence src binding to p32, suggesting accessory factors are key for stable membrane interactions.
Area of Science:
- Molecular Biology
- Cell Biology
- Virology
Background:
- pp60v-src is a myristylated transforming protein from Rous sarcoma virus.
- Its membrane association is a receptor-mediated process.
- Myristylated src peptides (MGYsrc) inhibit this association.
Purpose of the Study:
- To investigate the role of a candidate src receptor, p32, in pp60v-src membrane binding.
- To understand the relationship between MGYsrc peptide and pp60v-src polypeptide binding to membranes.
Main Methods:
- Cross-linking of radiolabeled MGYsrc peptide to fibroblast membranes.
- Identification of a 32-kilodalton (p32) membrane protein as a candidate src receptor.
- Analysis of subcellular membrane distribution of p32 and pp60v-src.
- In vitro experiments to assess inhibition of peptide cross-linking to p32 and pp60v-src membrane binding.
Main Results:
- p32's subcellular membrane distribution differs from pp60v-src in transformed cells.
- In vitro, MGYsrc peptide cross-linking to p32 could be inhibited without affecting pp60v-src membrane binding.
- Removing internal sequences from pp60v-src made its binding characteristics identical to MGYsrc peptide.
Conclusions:
- Internal membrane binding domains within pp60v-src influence its interaction with p32.
- Accessory binding factors may facilitate stable contact between pp60v-src and the cell membrane.