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Cited by 97

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

Adra, Chaker N., Manor, Danny, Ko, Jon L., Zhu, Shaochun, Horiuchi, Tadashi, Van Aelst, Linda, Cerione, Richard A., Lim, Bing·1997·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.94.9.4279
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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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Research works printed but not linked: 3

  1. Y Fukumoto, K Kaibuchi, Y Hori, H Fujiko, S Araki, T Ueda, A Kikuchi, Y Takai Oncogene 5, 1321–1328 (1990).
  2. K Takaishi, A Kikuchi, S Kuroda, K Kotani, T Sasaki, Y Takai Mol Cell Biol 13, 72–79 (1993).
  3. G Zalcman, V Closson, G Linares-Cruz, F Lerebours, N Honore, A Tavitian, B Olofsson Oncogene 10, 1935–1945 (1995).

Cited by

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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
DOI
10.1073/pnas.94.9.4279
Cited by
97
References
30
Language
en

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