Mechanistic principles of RAF kinase signaling
| Autor: | Marc Therrien, Frank Sicheri, Thanashan Rajakulendran, Christian M. Udell |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Pharmacology
MAPK/ERK pathway biology Kinase Protein domain Cell Biology Receptor tyrosine kinase Cell biology Protein–protein interaction Protein Structure Tertiary Cellular and Molecular Neuroscience Protein kinase domain Allosteric Regulation biology.protein Molecular Medicine Animals Humans raf Kinases c-Raf Signal transduction Molecular Biology Protein Kinases Signal Transduction |
| Zdroj: | Cellular and molecular life sciences : CMLS. 68(4) |
| ISSN: | 1420-9071 |
| Popis: | The RAF family of kinases are key components acting downstream of receptor tyrosine kinases and cells employ several distinct mechanisms to strictly control their activity. RAF transitions from an inactive state, where the N-terminal regulatory region binds intramolecularly to the C-terminal kinase domain, to an open state capable of executing the phosphoryl transfer reaction. This transition involves changes both within and between the protein domains in RAF. Many different proteins regulate the transition between inactive and active states of RAF, including RAS and KSR, which are arguably the two most prominent regulators of RAF function. Recent developments have added several new twists to our understanding of RAF regulation. Among others, dimerization of the RAF kinase domain is emerging as a crucial step in the RAF activation process. The multitude of regulatory protein–protein interactions involving RAF remains a largely untapped area for therapeutic applications. |
| Databáze: | OpenAIRE |
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