Related Experiment Videos
Clathrin-coated vesicles from human placenta contain GTP-binding proteins
J M Lenhard1, M A Levy, P D Stahl
1Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Biochemical and Biophysical Research Communications
|January 15, 1991
Summary
Researchers identified ras-like GTP-binding proteins in clathrin-coated vesicles. These proteins may regulate intracellular vesicle transport and signal transduction pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Clathrin-coated vesicles are essential for intracellular trafficking.
- The role of GTP-binding proteins in vesicle function is not fully understood.
Purpose of the Study:
- To investigate the presence and function of GTP-binding proteins in clathrin-coated vesicles.
- To identify specific GTP-binding proteins associated with coated vesicles.
Main Methods:
- Biochemical assays including GTP binding studies with [35S]GTP gamma S.
- Morphological techniques like electron microscopic autoradiography.
- Protein analysis using isoelectric focusing.
Main Results:
- Demonstrated GTP binding to clathrin coats and purified coated vesicles.
- Identified 23-24 kDa ras-like GTP-binding proteins within coated vesicles.
- Showed GTP and GTP gamma S inhibit [35S]GTP gamma S binding, suggesting specificity.
Conclusions:
- Low molecular weight GTP-binding proteins are present in clathrin-coated vesicles.
- These proteins likely play a regulatory role in vesicle-mediated transport.
- Potential involvement in signal transduction within intracellular organelles.