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The src protein contains multiple domains for specific attachment to membranes
J M Kaplan1, H E Varmus, J M Bishop
1G.W. Hooper Research Foundation, University of California Medical Center, San Francisco 94143.
Molecular and Cellular Biology
|March 1, 1990
Summary
The pp60src protein has distinct domains that direct it to specific cellular membranes, working with myristylation to control its location and function.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The pp60src protein, encoded by oncogenes v-src and c-src, associates with cellular membranes.
- This membrane association is partly due to N-terminal myristylation, but other protein regions are also implicated.
Purpose of the Study:
- To identify specific domains within pp60src responsible for membrane association and subcellular localization.
- To investigate the role of these domains in conjunction with myristylation.
Main Methods:
- Fusing various portions of pp60src to pyruvate kinase, a cytoplasmic protein.
- Analyzing the subcellular localization of these fusion proteins.
Main Results:
- Amino acids 1-14 of pp60src mediate myristylation and target pyruvate kinase to cytoplasmic granules.
- Amino acids 38-111 direct fusion proteins to the plasma and perinuclear membranes.
- Amino acids 204-259 primarily target proteins to perinuclear membranes.
Conclusions:
- pp60src possesses independent domains for membrane targeting and subcellular localization.
- These distinct domains likely contribute to the protein's diverse biological functions.