AI Article Synopsis
- RAF family kinases have been studied for over 30 years as key oncoproteins that relay signals from RAS and are linked to cancer.
- Recent findings reveal that RAF's catalytic activity relies on an allosteric mechanism involving kinase domain dimerization, which is important for understanding RAF's function.
- Current RAF inhibitors unexpectedly promote ERK signaling by encouraging RAF dimerization, indicating a need for more detailed structural studies of these kinases.
Article Abstract
RAF family kinases were among the first oncoproteins to be described more than 30 years ago. They primarily act as signalling relays downstream of RAS, and their close ties to cancer have fuelled a large number of studies. However, we still lack a systems-level understanding of their regulation and mode of action. The recent discovery that the catalytic activity of RAF depends on an allosteric mechanism driven by kinase domain dimerization is providing a vital new piece of information towards a comprehensive model of RAF function. The fact that current RAF inhibitors unexpectedly induce ERK signalling by stimulating RAF dimerization also calls for a deeper structural characterization of this family of kinases.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1038/nrm3979 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!