ArticleThe Journal of biological chemistry2013
Activated RhoA is a positive feedback regulator of the Lbc family of Rho guanine nucleotide exchange factor proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 57 citations in OpenAlex.
- Structural basis for membrane-dependent positive feedback regulation of DOCK11 by activated Cdc42.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Mechanisms by Which RhoA Activity and Associated Synaptic Effects Are Controlled by the DISC1 Scaffolding-Like Protein.Biological psychiatry · 2026Article
- Endogenous OptoRhoGEFs reveal biophysical principles of epithelial tissue furrowing.Nature communications · 2025Article
- Optogenetic control of a GEF of RhoA uncovers a signaling switch from retraction to protrusion.eLife · 2025Article
- Identification ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- RhoJ: an emerging biomarker and target in cancer research and treatment.Cancer gene therapy · 2024Review
- Excitable Rho dynamics control cell shape and motility by sequentially activating ERM proteins and actomyosin contractility.Science advances · 2024Article
- Non-canonical Wnt signaling triggered by WNT2B drives adrenal aldosterone production.bioRxiv : the preprint server for biology · 2024Article
- New Mechanisms Underlying Oncogenesis in Dbl Family Rho Guanine Nucleotide Exchange Factors.Molecular pharmacology · 2024Review
- Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024Review
- Direct investigation of cell contraction signal networks by light-based perturbation methods.Pflugers Archiv : European journal of physiology · 2023Review
- An AMPK phosphoregulated RhoGEF feedback loop tunes cortical flow-driven amoeboid migration in vivo.Science advances · 2022Article
- Monitoring the Response of Multiple Signal Network Components to Acute Chemo-Optogenetic Perturbations in Living Cells.Chembiochem : a European journal of chemical biology · 2022Article
- Stochasticity and positive feedback enable enzyme kinetics at the membrane to sense reaction size.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Optogenetic Tuning Reveals Rho Amplification-Dependent Dynamics of a Cell Contraction Signal Network.Cell reports · 2020Article
- Rho1 activation recapitulates early gastrulation events in the ventral, but not dorsal, epithelium ofeLife · 2020Article
- Structure and regulation of human epithelial cell transforming 2 protein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural Insights into the Regulation Mechanism of Small GTPases by GEFs.Molecules (Basel, Switzerland) · 2019Review
- In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation.eLife · 2019Article
- Autoactivation of small GTPases by the GEF-effector positive feedback modules.F1000Research · 2019Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The monomeric Rho GTPases are essential for cellular regulation including cell architecture and movement. A direct mechanism for hormonal regulation of the RhoA-type GTPases is their modulation by the G12 and G13 proteins via RH (RGS homology) containing RhoGEFs. In addition to the interaction of the G protein α subunits with the RH domain, activated RhoA also binds to the pleckstrin homology (PH) domain of PDZRhoGEF. The latter interaction is now extended to all seven members of the homologous Lbc family of RhoGEFs which includes the RH-RhoGEFs. This is evinced by direct measurements of binding or through effects on selected signaling pathways in cells. Overexpression of these PH domains alone can block RhoA-dependent signaling in cells to various extents. Whereas activated RhoA does not modulate the intrinsic activity of the RhoGEFs, activated RhoA associated with phospholipid vesicles can facilitate increased activity of soluble RhoGEFs on vesicle-delimited substrate (RhoA-GDP). This demonstrates feasibility of the hypothesis that binding of activated RhoA to the PH domains acts as a positive feedback mechanism. This is supported by cellular studies in which mutation of this binding site on PH strongly attenuates the stimulation of RhoA observed by overexpression of five of the RhoGEF DH-PH domains. This mutation is even more dramatic in the context of full-length p115RhoGEF. The utilization of this mechanism by multiple RhoGEFs suggests that this regulatory paradigm may be a common feature in the broader family of RhoGEFs.
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