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Molecular complexes that contain both c-Cbl and c-Src associate with Golgi membranes
Frederic Bard1, Urjeet Patel, Joan B Levy
1Department of Orthopaedics, Yale University School of Medicine, New Haven, CT 06520-8044, USA.
European Journal of Cell Biology
|March 15, 2002
Summary
Cbl protein associates with Golgi membranes and interacts with activated Src kinase. This interaction at the Golgi may regulate Golgi function, impacting cellular signaling pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Signal Transduction
Background:
- Cbl is an adaptor protein involved in receptor tyrosine kinase regulation.
- Cbl acts as a kinase inhibitor and E3 ubiquitin ligase, mediating receptor down-regulation.
- Cbl translocates to intracellular compartments upon receptor activation.
Purpose of the Study:
- To investigate the association of Cbl protein with Golgi membranes.
- To explore the interaction of Cbl with Src kinase at the Golgi.
- To understand the functional implications of Cbl localization at the Golgi.
Main Methods:
- Confocal immunofluorescence staining to visualize Cbl and Golgi markers.
- Subcellular fractionation using density centrifugation and free-flow electrophoresis.
- Co-immunoprecipitation assays to detect protein interactions.
Main Results:
- Cbl colocalizes with Golgi markers in unstimulated cells.
- A fraction of Cbl is stably associated with Golgi-enriched membranes.
- Membrane-bound Cbl is hyperphosphorylated and co-immunoprecipitates with Src.
- Activated Src enhances Cbl association with Golgi membranes.
Conclusions:
- Cbl localizes to Golgi membranes and forms a complex with activated Src.
- This Golgi-associated Cbl-Src complex may play a role in regulating Golgi function.
- The findings suggest a novel regulatory mechanism involving Cbl at the Golgi apparatus.