RhoA regulation in space and time
Open accessAbstract
RhoGTPases are well known for being controllers of cell cytoskeleton and share common features in the way they act and are controlled. These include their switch from GDP to GTP states, their regulations by different guanine exchange factors (GEFs), GTPase‐activating proteins and guanosine dissociation inhibitors (GDIs), and their similar structure of active sites/membrane anchors. These very similar features often lead to the common consideration that the differences in their biological effects mainly arise from the different types of regulators and specific effectors associated with each GTPase. Focusing on data obtained through biosensors, live cell microscopy and recent optogenetic approaches, we highlight in this review that the regulation of RhoA appears to depart from Cdc42 and Rac1 modes of regulation through its enhanced lability at the plasma membrane. RhoA presents a high dynamic turnover at the membrane that is regulated not only by GDIs but also by GEFs, effectors and a possible soluble conformational state. This peculiarity of RhoA regulation may be important for the specificities of its functions, such as the existence of activity waves or its putative dual role in the initiation of protrusions and contractions.
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RhoA activation is primarily restricted to the plasma membrane.
“Sequestration of GEF-H1 on microtubules can effectively regulate its activity, because RhoA activation is primarily restricted to the plasma membrane 30 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [30]
The Conclusions and perspectives section (Fig. 7; page not specified in our copy) says active RhoA preferentially binds the plasma membrane and has its highest potential to activate downstream pathways there. But the same section says RhoA can be GTP-bound in both the cytoplasm and at the membrane, so describing its activation as primarily restricted to the membrane overstates the spatial restriction. (LLM, conf=0.87)
Experimental — accuracy not yet measuredSequestration of GEF-H1 on microtubules can effectively regulate its activity.
“Sequestration of GEF-H1 on microtubules can effectively regulate its activity, because RhoA activation is primarily restricted to the plasma membrane 30 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [30]
The optogenetic-approaches section (p. 844) reports that sequestering a GEF domain on mitochondria decreased contractility, and that recruiting GEF domains, including GEF-H1, to the plasma membrane activated RhoA. It does not establish that sequestration of GEF-H1 on microtubules regulates its activity. The conclusions also say RhoA can be GTP-bound in the cytoplasm, so the paper does not describe its activation as restricted to the plasma membrane. (LLM, conf=0.84)
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- Authors
- de Seze, J., Gatin, J., & Coppey, M.
- Affiliations
- Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico‐Chimie Curie Paris France
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Coppey, Mathieu
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2023-01-29
- Volume
- 597
- Issue
- 6
- Pages
- 836-849
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W4317519889
- Cited by
- 42
- References
- 72
- Citations by year
- 2026: 15 · 2025: 9 · 2024: 8 · 2023: 10
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Update notices
- correction (2023-06-27)
- Open access
- hybrid
- doi.org
- Licence
- Locations
- FEBS Letters (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Agence Nationale de la Recherche (ANR‐10‐IDEX‐0001‐02, ANR‐18‐0013‐02, ANR‐11‐LABX‐0038, ANR10‐INBS‐04, ANR‐17‐CONV‐0005)
- Institut Curie
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- RhoA, Rho GTPases, guanine nucleotide exchange factor, GTPase-activating protein, plasma membrane, cytoskeleton regulation, cell protrusions, cell contraction, optogenetics, live-cell imaging, biosensors
- MeSH terms
- Guanine Nucleotide Exchange Factors, GTPase-Activating Proteins, Guanine Nucleotide Dissociation Inhibitors, rhoA GTP-Binding Protein
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