The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
Abstract
Mammalian DOCK180 protein and its orthologues Myoblast City (MBC) and CED-5 in Drosophila and Caenorhabditis elegans, respectively,function as critical regulators of the small GTPase Rac during several fundamentally important biological processes, such as cell motility and phagocytosis. The mechanism by which DOCK180 and its orthologues regulate Rac has remained elusive. We report here the identification of a domain within DOCK180 named DHR-2 (Dock Homology Region-2)that specifically binds to nucleotide-free Rac and activates Rac in vitro. Our studies further demonstrate that the DHR-2 domain is both necessary and sufficient for DOCK180-mediated Rac activation in vivo. Importantly, we have identified several novel homologues of DOCK180 that possess this domain and found that many of them directly bind to and exchange GDP for GTP both in vitro and in vivo on either Rac or another Rho-family member, Cdc42. Our studies therefore identify a novel protein domain that interacts with and activates GTPases and suggest the presence of an evolutionarily conserved DOCK180-related superfamily of exchange factors.
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Cites
Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
Brugnera, E., Haney, L., Grimsley, C., Lu, M., Walk, S. F., Tosello-Trampont, A.-C., Macara, I. G., Madhani, H., Fink, G. R., & Ravichandran, K. S. (2002) · Nature Cell Biology · doi:10.1038/ncb824 · Cited by 576
A motif-based profile scanning approach for genome-wide prediction of signaling pathways
Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., & Cantley, L. C. (2001) · Nature Biotechnology · doi:10.1038/86737 · Cited by 517
Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
Fukui, Y., Hashimoto, O., Sanui, T., Oono, T., Koga, H., Abe, M., Inayoshi, A., Noda, M., Oike, M., Shirai, T., et al. (2001) · Nature · doi:10.1038/35090591 · Cited by 449
Rossman, K. L., Worthylake, D. K., Snyder, J. T., Siderovski, D. P., Campbell, S. L., & Sondek, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.6.1315 · Cited by 222
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
Meller, N., Irani-Tehrani, M., Kiosses, W. B., Del Pozo, M. A., & Schwartz, M. A. (2002) · Nature Cell Biology · doi:10.1038/ncb835 · Cited by 171
Trp56 of Rac1 Specifies Interaction with a Subset of Guanine Nucleotide Exchange Factors
Gao, Y., Xing, J., Streuli, M., Leto, T. L., & Zheng, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108865200 · Cited by 115
A novel mechanism for the regulation of amyloid precursor protein metabolism
Chen, Q., Kimura, H., & Schubert, D. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110151 · Cited by 63
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Burridge, K., & Wennerberg, K. (2004) · Cell · doi:10.1016/s0092-8674(04)00003-0 · Cited by 1,578
Cell migration: Rho GTPases lead the way
Raftopoulou, M., & Hall, A. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2003.06.003 · Cited by 1,235
Mechanical Integration of Actin and Adhesion Dynamics in Cell Migration
Gardel, M. L., Schneider, I. C., Aratyn-Schaus, & Waterman, C. M. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.011209.122036 · Cited by 981
Rac Activation and Inactivation Control Plasticity of Tumor Cell Movement
Sanz-Moreno, V., Gadea, G., Ahn, J., Paterson, H., Marra, P., Pinner, S., Sahai, E., & Marshall, C. J. (2008) · Cell · doi:10.1016/j.cell.2008.09.043 · Cited by 959
Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?
Vigil, D., Cherfils, J., Rossman, K. L., & Der, C. J. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2960 · Cited by 819
Metadata
- Authors
- Côté, J.-F., & Vuori, K.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2002-12-15
- Volume
- 115
- Issue
- 24
- Pages
- 4901-4913
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2122108815
- Cited by
- 415
- References
- 7
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- closed
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