The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
RhoGDIγ: A GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas
Abstract
GDP-dissociation inhibitors (GDIs) play a primary role in modulating the activation of GTPases and may also be critical for the cellular compartmentalization of GTPases. RhoGDI and GDI/D4 are two currently known GDIs for the Rho-subfamily of GTPases. Using their cDNAs to screen a human brain cDNA library under low stringency, we have cloned a homologous cDNA preferentially expressed at high levels in brain and pancreas. The predicted protein, named RhoGDIγ, is ≈50% identical to GDI/D4 and RhoGDI. It binds to CDC42 and RhoA with less affinity compared with RhoGDI and does not bind with Rac1, Rac2, or Ras. RhoGDIγ functions as a GDI for CDC42 but with ≈20 times less efficiency than RhoGDI. Immunohistochemical studies showed a diffuse punctate distribution of the protein in the cytoplasm with concentration around the nucleus in cytoplasmic vesicles. Overexpression of the protein in baby hamster kidney cells caused the cells to round up with loss of stress fibers. A distinct hydrophobic amino terminus in RhoGDIγ, not seen in the other two RhoGDIs, could provide a mechanism for localization of the GDI to specific membranous compartment thus determining function distinct from RhoGDI or GDI/D4. Our results provide evidence that there is a family of GDIs for the Rho-related GTPases and that they differ in binding affinity, target specificity, and tissue expression. We propose that RhoGDI be renamed RhoGDIα and GDID4 be renamed RhoGDIβ. The new GDI should widen the scope of investigation of this important class of regulatory protein.
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“Athird regulatory protein that is involved in GTPase activity is the GDI (2, 32, 59).”
From The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient and Modulates Activities of Other Rho GTPases by an Inhibitory Function (2002) · cites this paper as [2]
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“In vitro assays have shown that GDIs inhibit GDPdissociation and compete with GEF for activation of Rho GTPases (2, 32).”
From The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient and Modulates Activities of Other Rho GTPases by an Inhibitory Function (2002) · cites this paper as [2]
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Cited by
Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
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Metadata
- Authors
- Adra, C. N., Manor, D., Ko, J. L., Zhu, S., Horiuchi, T., Van Aelst, L., Cerione, R. A., & Lim, B.
- Affiliations
- Harvard Institutes of Medicine, HIM955, Beth Israel Hospital, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215; Department of Pharmacology, Veterinary Teaching Hospital, Cornell University, Ithaca, NY 14853; and Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1997-04-29
- Volume
- 94
- Issue
- 9
- Pages
- 4279-4284
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 97
- References
- 30
- Language
- en
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- Adra, C. N., Manor, D., Ko, J. L., Zhu, S., Horiuchi, T., Van Aelst, L., Cerione, R. A., & Lim, B. (1997). RhoGDIγ: A GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.9.4279
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