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Gene Review

RHO3  -  Rho family GTPase RHO3

Saccharomyces cerevisiae S288c

Synonyms: GTP-binding protein RHO3, YIL118W
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High impact information on RHO3

  • Our analysis of a Rho3 mutant that is unable to interact with the Exo70 subunit of the exocyst reveals a normal polarization of the exocyst complex as well as other polarity markers [1].
  • Consistent with this model, we find that the ability of Rho3 and Cdc42 to hydrolyze GTP is not required for their role in secretion [1].
  • We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins [2].
  • Extensive genetic interactions between cdc42-6 and mutations in exocytic components support this hypothesis, and indicate a functional overlap with Rho3, which also regulates both actin organization and exocytosis [3].
  • Genetic analysis suggests that Sro7 and Sec9 function together in a pathway downstream of the Rho3 GTPase [4].

Biological context of RHO3


Anatomical context of RHO3


Associations of RHO3 with chemical compounds

  • Furthermore, the growth of T. reesei was not affected on glucose by the rho3 disruption [11].

Regulatory relationships of RHO3

  • The non-essential RGD1 gene from Saccharomyces cerevisiae encodes a protein that has been characterized in vitro as a Rho GTPase activating protein (RhoGAP) for the Rho3 and Rho4 proteins [12].

Other interactions of RHO3

  • Analysis of the synthetic lethal phenomenon revealed that production of activated Rho3p and Rho4p leads to lethality in wsc1Delta cells [5].
  • Rgd1, a GTPase-activating protein, is the only known negative regulator of the Rho3 and Rho4 small GTPases in the yeast Saccharomyces cerevisiae [5].
  • Consistent with this idea, it was found that perturbations in Rho3-mediated polarized exocytosis specifically impair the abundance and processing of Wsc1 and Mid2 proteins [5].
  • Overlapping subcellular localization of the Rho3 and Exo70 proteins was demonstrated by indirect immunofluorescence [7].
  • Yeast SRO7 was identified as a multicopy suppressor of a defect in Rho3p, a small GTPase that maintains cell polarity [13].


  1. Rho GTPase regulation of exocytosis in yeast is independent of GTP hydrolysis and polarization of the exocyst complex. Roumanie, O., Wu, H., Molk, J.N., Rossi, G., Bloom, K., Brennwald, P. J. Cell Biol. (2005) [Pubmed]
  2. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. Dong, Y., Pruyne, D., Bretscher, A. J. Cell Biol. (2003) [Pubmed]
  3. Yeast Cdc42 functions at a late step in exocytosis, specifically during polarized growth of the emerging bud. Adamo, J.E., Moskow, J.J., Gladfelter, A.S., Viterbo, D., Lew, D.J., Brennwald, P.J. J. Cell Biol. (2001) [Pubmed]
  4. Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. Lehman, K., Rossi, G., Adamo, J.E., Brennwald, P. J. Cell Biol. (1999) [Pubmed]
  5. The Rho3 and Rho4 small GTPases interact functionally with Wsc1p, a cell surface sensor of the protein kinase C cell-integrity pathway in Saccharomyces cerevisiae. Fernandes, H., Roumanie, O., Claret, S., Gatti, X., Thoraval, D., Doignon, F., Crouzet, M. Microbiology (Reading, Engl.) (2006) [Pubmed]
  6. Yeast src homology region 3 domain-binding proteins involved in bud formation. Matsui, Y., Matsui, R., Akada, R., Toh-e, A. J. Cell Biol. (1996) [Pubmed]
  7. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Robinson, N.G., Guo, L., Imai, J., Toh-E, A., Matsui, Y., Tamanoi, F. Mol. Cell. Biol. (1999) [Pubmed]
  8. Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast. Aronov, S., Gerst, J.E. J. Biol. Chem. (2004) [Pubmed]
  9. The protein kinase Kic1 affects 1,6-beta-glucan levels in the cell wall of Saccharomyces cerevisiae. Vink, E., Vossen, J.H., Ram, A.F., van den Ende, H., Brekelmans, S., de Nobel, H., Klis, F.M. Microbiology (Reading, Engl.) (2002) [Pubmed]
  10. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Adamo, J.E., Rossi, G., Brennwald, P. Mol. Biol. Cell (1999) [Pubmed]
  11. Interactions of the Trichoderma reesei rho3 with the secretory pathway in yeast and T. reesei. Vasara, T., Salusjärvi, L., Raudaskoski, M., Keränen, S., Penttilä, M., Saloheimo, M. Mol. Microbiol. (2001) [Pubmed]
  12. Evidence for the genetic interaction between the actin-binding protein Vrp1 and the RhoGAP Rgd1 mediated through Rho3p and Rho4p in Saccharomyces cerevisiae. Roumanie, O., Peypouquet, M.F., Bonneu, M., Thoraval, D., Doignon, F., Crouzet, M. Mol. Microbiol. (2000) [Pubmed]
  13. Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function. Kagami, M., Toh-e, A., Matsui, Y. Genetics (1998) [Pubmed]
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