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Beyond the RING: CBL proteins as multivalent adapters
A Y Tsygankov1, A M Teckchandani, E A Feshchenko
1Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Pennsylvania, PA 19140, USA. tsygan@astro.temple.edu
Abstract:
Following discovery of c-Cbl, a cellular form of the transforming retroviral protein v-Cbl, multiple Cbl-related proteins have been identified in vertebrate and invertebrate organisms. c-Cbl and its homologues are capable of interacting with numerous proteins involved in cell signaling, including various molecular adapters and protein tyrosine kinases. It appears that Cbl proteins play several functional roles, acting both as multivalent adapters and inhibitors of various protein tyrosine kinases. The latter function is linked, to a substantial extent, to the E3 ubiquitin-ligase activity of Cbl proteins. Experimental evidence for these functions, interrelations between them, and their biological significance are addressed in this review, with the main accent placed on the adapter functions of Cbl proteins.
Insights
The Cbl protein family acts as crucial cell signaling adapters and inhibitors of protein tyrosine kinases. Their E3 ubiquitin-ligase activity is key to these functions, impacting various biological processes.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- Discovery of c-Cbl, a cellular homolog of v-Cbl, revealed a family of related proteins.
- Cbl proteins interact with diverse signaling molecules, including protein tyrosine kinases and molecular adapters.
Purpose of the Study:
- To review the functional roles of Cbl proteins.
- To highlight their significance as multivalent adapters and inhibitors of protein tyrosine kinases.
- To emphasize the role of E3 ubiquitin-ligase activity in Cbl protein function.
Main Methods:
- Literature review of experimental evidence.
- Analysis of Cbl protein interactions.
- Examination of E3 ubiquitin-ligase activity.
Main Results:
- Cbl proteins function as multivalent adapters in cell signaling pathways.
- They act as inhibitors of various protein tyrosine kinases.
- E3 ubiquitin-ligase activity is substantially linked to their inhibitory function.
Conclusions:
- Cbl proteins are versatile regulators of cell signaling.
- Their adapter functions are central to their biological roles.
- Understanding Cbl proteins is crucial for comprehending cell signaling networks.