The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
The Role of Rho in G Protein-Coupled Receptor Signal Transduction
Abstract
Low molecular weight G proteins of the Rho subfamily are regulators of actin cytoskeletal organization. In contrast to the heterotrimeric G proteins, the small GTPases are not directly activated through ligand binding to G protein–coupled receptors (GPCRs). However, a subset of GPCRs, including those for lysophosphatidic acid and thrombin, induce stress fibers, focal adhesions, and cell rounding through Rho-dependent pathways. C3 exoenzyme has been a useful tool for demonstrating Rho involvement in these and other responses, including Ca 2+sensitization of smooth muscle contraction, cell migration, transformation, and serum response element–mediated gene expression. Most of the GPCRs that induce Rho-dependent responses can activate G q, but this is not a sufficient signal. Recent data demonstrate that Gα 12/13 can induce Rho-dependent responses. Furthermore, Gα 12/13 can bind and activate Rho-specific guanine nucleotide exchange factors, providing a mechanism by which GPCRs that couple to Gα 12/13 could activate Rho and its downstream responses.
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Cites
Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
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Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
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A role for Rho in Ras transformation
Qiu, R. G., Chen, J., McCormick, F., & Symons, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11781 · Cited by 533
Rho family proteins and Ras transformation: the RHOad less traveled gets congested
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GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors
Rossman, K. L., Der, C. J., & Sondek, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1587 · Cited by 1,697
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Nichols, D. E., & Nichols, C. D. (2008) · Chemical Reviews · doi:10.1021/cr078224o · Cited by 895
Jiang, L. I., Collins, J., Davis, R., Lin, K.-M., DeCamp, D., Roach, T., Hsueh, R., Rebres, R. A., Ross, E. M., Taussig, R., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609695200 · Cited by 358
Metadata
- Authors
- Sah, V. P., Seasholtz, T. M., Sagi, S. A., & Brown, J. H.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2000-04
- Volume
- 40
- Issue
- 1
- Pages
- 459-489
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2163133008
- Cited by
- 348
- References
- 6
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
