Abstract
Rho GTPases regulate cytoskeletal and cell adhesion dynamics and thereby coordinate a wide range of cellular processes, including cell migration, cell polarity and cell cycle progression. Most Rho GTPases cycle between a GTP-bound active conformation and a GDP-bound inactive conformation to regulate their ability to activate effector proteins and to elicit cellular responses. However, it has become apparent that Rho GTPases are regulated by post-translational modifications and the formation of specific protein complexes, in addition to GTP-GDP cycling. The canonical regulators of Rho GTPases - guanine nucleotide exchange factors, GTPase-activating proteins and guanine nucleotide dissociation inhibitors - are regulated similarly, creating a complex network of interactions to determine the precise spatiotemporal activation of Rho GTPases.
Original language | English |
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Pages (from-to) | 496-510 |
Number of pages | 15 |
Journal | Nature Reviews Molecular Cell Biology |
Volume | 17 |
Issue number | 8 |
Early online date | 15 Jun 2016 |
DOIs | |
Publication status | Published - Aug 2016 |
Keywords
- Animals
- Humans
- Protein Processing, Post-Translational
- rho GTP-Binding Proteins
- Journal Article
- Review