The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Regulation of the Cytoskeleton and Cell Adhesion by the Rho Family GTPases in Mammalian Cells
Abstract
▪ Abstract Members of the Rho family of small Ras-like GTPases—including RhoA, -B, and -C, Rac1 and -2, and Cdc42—exhibit guanine nucleotide-binding activity and function as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state. The Rho family GTPases participate in regulation of the actin cytoskeleton and cell adhesion through specific targets. Identification and characterization of these targets have begun to clarify how the Rho family GTPases act to regulate cytoskeletal structure and cell-cell and cell-substratum contacts in mammalian cells. The Rho family GTPases are also involved in regulation of smooth muscle contraction, cell morphology, cell motility, neurite retraction, and cytokinesis. However, the molecular mechanisms by which the Rho family GTPases participate in the regulation of such processes are not well established.
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Citations
Cites
Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
Amano, M., Chihara, K., Kimura, K., Fukata, Y., Nakamura, N., Matsuura, Y., & Kaibuchi, K. (1997) · Science · doi:10.1126/science.275.5304.1308 · Cited by 1,077
Self-citationActivation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S., & Der, C. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6443 · Cited by 683
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
Structural and Functional Regulation of Tight Junctions by RhoA and Rac1 Small GTPases
Jou, T.-S., Schneeberger, E. E., & James Nelson, W. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.101 · Cited by 354
p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase
Kobayashi, K., Kuroda, S., Fukata, M., Nakamura, T., Nagase, T., Nomura, N., Matsuura, Y., Yoshida-Kubomura, N., Iwamatsu, A., & Kaibuchi, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.291 · Cited by 244
Self-citation
Cited by
Rho‐kinase/ROCK: A key regulator of the cytoskeleton and cell polarity
Amano, M., Nakayama, M., & Kaibuchi, K. (2010) · Cytoskeleton · doi:10.1002/cm.20472 · Cited by 994
Self-citationHabas, R., Kato, Y., & He, X. (2001) · Cell · doi:10.1016/s0092-8674(01)00614-6 · Cited by 842
Actin Cytoskeleton Regulation in Neuronal Morphogenesis and Structural Plasticity
Luo, L. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.031802.150501 · Cited by 658
Coactivation of Rac and Rho by Wnt/Frizzled signaling is required for vertebrate gastrulation
Habas, R., Dawid, I. B., & He, X. (2003) · Genes & Development · doi:10.1101/gad.1022203 · Cited by 603
Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
Wang, H.-R., Zhang, Y., Ozdamar, B., Ogunjimi, A. A., Alexandrova, E., Thomsen, G. H., & Wrana, J. L. (2003) · Science · doi:10.1126/science.1090772 · Cited by 551
Metadata
- Authors
- Kaibuchi, K., Kuroda, S., & Amano, M.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1999-06
- Volume
- 68
- Issue
- 1
- Pages
- 459-486
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2162049443
- Cited by
- 1,017
- References
- 5
- FWCI
- 4.52
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kaibuchi, K., Kuroda, S., & Amano, M. (1999). Regulation of the Cytoskeleton and Cell Adhesion by the Rho Family GTPases in Mammalian Cells. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.68.1.459
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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.
