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Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1

Boulter, Etienne, Garcia-Mata, Rafael, Guilluy, Christophe, Dubash, Adi, Rossi, Guendalina, Brennwald, Patrick J., Burridge, Keith·2010·Nature Cell Biology
DOI 10.1038/ncb2049PMC PMC2866742
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Research works printed but not linked: 28

  1. DerMardirossian, C. & Bokoch, G. M. GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15, 356–363 (2005). · DOI
  2. Dransart, E., Morin, A., Cherfils, J. & Olofsson, B. Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors. J. Biol. Chem. 280, 4674–4683 (2005). · DOI
  3. Gorovoy, M. et al. RhoGDI-1 modulation of the activity of monomeric RhoGTPase RhoA regulates endothelial barrier function in mouse lungs. Circ. Res. 101, 50–58 (2007). · DOI
  4. Abe, M., Qadota, H., Hirata, A. & Ohya, Y. Lack of GTP-bound Rho1p in secretory vesicles of Saccharomyces cerevisiae. J. Cell Biol. 162, 85–97 (2003). · DOI
  5. Tong, Z. et al. Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition. J. Cell Biol. 179, 1375–1384 (2007). · DOI
  6. Togawa, A. et al. Progressive impairment of kidneys and reproductive organs in mice lacking Rho GDIα. Oncogene 18, 5373–5380 (1999). · DOI
  7. Shibata, S. et al. Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease. Nature Med. 14, 1370–1376 (2008). · DOI
  8. Bielek, H., Anselmo, A. & Dermardirossian, C. Morphological and proliferative abnormalities in renal mesangial cells lacking RhoGDI. Cell Signal. 21, 1974–1983 (2009). · DOI
  9. Tiedje, C., Sakwa, I., Just, U. & Hofken, T. The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms. Mol. Biol. Cell 19, 2885–2896 (2008). · DOI
  10. Winter-Vann, A. M. & Casey, P. J. Post-prenylation-processing enzymes as new targets in oncogenesis. Nature Rev. Cancer 5, 405–412 (2005). · DOI · Paper page
  11. Doye, A. et al. CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion. Cell 111, 553–564 (2002). · DOI
  12. Vega, F. M. & Ridley, A. J. SnapShot: Rho family GTPases. Cell 129, 1430 (2007). · DOI
  13. Shao, F. et al. Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc. Natl Acad. Sci. USA 100, 904–909 (2003). · DOI
  14. Young, J. C., Agashe, V. R., Siegers, K. & Hartl, F. U. Pathways of chaperone-mediated protein folding in the cytosol. Nature Rev. Mol. Cell Biol. 5, 781–791 (2004). · DOI
  15. Michaelson, D. et al. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152, 111–126 (2001). · DOI · Paper page
  16. Hart, M. J. et al. A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs. Science 258, 812–815 (1992). · DOI · Paper page
  17. Ueda, T., Kikuchi, A., Ohga, N., Yamamoto, J. & Takai, Y. Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein. J. Biol. Chem. 265, 9373–9380 (1990). · DOI · Paper page
  18. Clark, E. A., Golub, T. R., Lander, E. S. & Hynes, R. O. Genomic analysis of metastasis reveals an essential role for RhoC. Nature 406, 532–535 (2000). · DOI
  19. Guthrie, C., Fink, G., Simon, M. I. & Abelson, J. N. Guide to yeast genetics and molecular biology. Methods Enzymol. 194, 1–863 (1991).
  20. Adamo, J. E. et al. Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud. J. Cell Biol. 155, 581–592 (2001). · DOI
  21. Garcia-Mata, R. et al. Analysis of activated GAPs and GEFs in cell lysates. Methods Enzymol. 406, 425–437 (2006). · DOI
  22. Wennerberg, K. et al. RhoG signals in parallel with Rac1 and Cdc42. J. Biol. Chem. 277, 47810–47817 (2002). · DOI
  23. Arthur, W. T., Noren, N. K. & Burridge, K. Regulation of Rho family GTPases by cell–cell and cell–matrix adhesion. Biol. Res. 35, 239–246 (2002). · DOI
  24. van Buul, J. D. et al. RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration. J. Cell Biol. 178, 1279–1293 (2007). · DOI
  25. Huesken, D. et al. Design of a genome-wide siRNA library using an artificial neural network. Nature Biotechnol. 23, 995–1001 (2005). · DOI
  26. Vouret-Craviari, V., Boulter, E., Grall, D., Matthews, C. & Van Obberghen-Schilling, E. ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells. J. Cell Sci. 117, 4559–4569 (2004). · DOI
  27. Bagrodia, S., Taylor, S. J., Jordon, K. A., Van Aelst, L. & Cerione, R. A. A novel regulator of p21-activated kinases. J. Biol. Chem. 273, 23633–23636 (1998). · DOI
  28. Ren, X. D., Kiosses, W. B. & Schwartz, M. A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578–585 (1999). · DOI

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Metadata

Authors
Boulter, E., Garcia-Mata, R., Guilluy, C., Dubash, A., Rossi, G., Brennwald, P. J., & Burridge, K.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2010-04-18
Volume
12
Issue
5
Pages
477-483
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/ncb2049
PMC
PMC2866742
Cited by
346
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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CoChat. (2026). Citation check: Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1. https://app.cochat.ai/papers/10.1038/ncb2049
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Boulter, E., Garcia-Mata, R., Guilluy, C., Dubash, A., Rossi, G., Brennwald, P. J., & Burridge, K. (2010). Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1. Nature Cell Biology. https://doi.org/10.1038/ncb2049