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Gene Review

RHOD  -  ras homolog family member D

Homo sapiens

Synonyms: ARHD, RHOHP1, RHOM, Rho, Rho-related GTP-binding protein RhoD, ...
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Disease relevance of RHOD


Psychiatry related information on RHOD


High impact information on RHOD


Chemical compound and disease context of RHOD


Biological context of RHOD


Anatomical context of RHOD

  • Here, we identify a novel splice variant of human Diaphanous, hDia2C, which specifically binds to RhoD and is recruited onto early endosomes [19].
  • Thus, this deamidation of glutamine 63 by CNF1 leads to the constitutive activation of Rho, and induces the reorganization of actin stress fibres [23].
  • The assembly of focal adhesions is regulated by the GTP-binding protein Rho [24].
  • Studies in different areas such as cell migration, mitosis, and asymmetric cell division have shown that Ran, Rho, and heterotrimeric G proteins regulate many aspects of microtubule functions [25].
  • In contrast to these well established effects of Rho and Rac on plasma membrane morphology and bulk pinocytosis, there has been no evidence for their involvement in the regulation of receptor-mediated endocytosis in clathrin-coated pits [26].

Associations of RHOD with chemical compounds


Physical interactions of RHOD

  • Here we show that, of a large number of GTPases tested, only Rnd1 and RhoD bind the cytoplasmic domain of Plexin-A1 [29].

Other interactions of RHOD

  • The underlying molecular basis for these effects of Rho proteins are incompletely understood, but in the case of Cdc42 it appears that it can drive vesicle movement through Arp2/3 complex-mediated actin polymerization at the surface of the vesicle [30].
  • Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse [29].

Analytical, diagnostic and therapeutic context of RHOD


  1. Mutations in ARHGEF6, encoding a guanine nucleotide exchange factor for Rho GTPases, in patients with X-linked mental retardation. Kutsche, K., Yntema, H., Brandt, A., Jantke, I., Nothwang, H.G., Orth, U., Boavida, M.G., David, D., Chelly, J., Fryns, J.P., Moraine, C., Ropers, H.H., Hamel, B.C., van Bokhoven, H., Gal, A. Nat. Genet. (2000) [Pubmed]
  2. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Servant, G., Weiner, O.D., Herzmark, P., Balla, T., Sedat, J.W., Bourne, H.R. Science (2000) [Pubmed]
  3. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Maekawa, M., Ishizaki, T., Boku, S., Watanabe, N., Fujita, A., Iwamatsu, A., Obinata, T., Ohashi, K., Mizuno, K., Narumiya, S. Science (1999) [Pubmed]
  4. Caenorhabditis elegans LET-502 is related to Rho-binding kinases and human myotonic dystrophy kinase and interacts genetically with a homolog of the regulatory subunit of smooth muscle myosin phosphatase to affect cell shape. Wissmann, A., Ingles, J., McGhee, J.D., Mains, P.E. Genes Dev. (1997) [Pubmed]
  5. Direct modulation of the host cell cytoskeleton by Salmonella actin-binding proteins. Hayward, R.D., Koronakis, V. Trends Cell Biol. (2002) [Pubmed]
  6. Rho is a presynaptic activator of neurotransmitter release at pre-existing synapses in C. elegans. McMullan, R., Hiley, E., Morrison, P., Nurrish, S.J. Genes Dev. (2006) [Pubmed]
  7. Ras family therapy: Rab, Rho and Ral talk to the exocyst. Novick, P., Guo, W. Trends Cell Biol. (2002) [Pubmed]
  8. The neurite retraction induced by lysophosphatidic acid increases Alzheimer's disease-like Tau phosphorylation. Sayas, C.L., Moreno-Flores, M.T., Avila, J., Wandosell, F. J. Biol. Chem. (1999) [Pubmed]
  9. Rho GTPases, dendritic structure, and mental retardation. Newey, S.E., Velamoor, V., Govek, E.E., Van Aelst, L. J. Neurobiol. (2005) [Pubmed]
  10. Neurophysiology/pharmacology of erection. Andersson, K.E. Int. J. Impot. Res. (2001) [Pubmed]
  11. Phospholipase D: enzymology, mechanisms of regulation, and function. Exton, J.H. Physiol. Rev. (1997) [Pubmed]
  12. Rho and Rac take center stage. Burridge, K., Wennerberg, K. Cell (2004) [Pubmed]
  13. Muscle or fat? Rho bridges the GAP. Saltiel, A.R. Cell (2003) [Pubmed]
  14. Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1. Habas, R., Kato, Y., He, X. Cell (2001) [Pubmed]
  15. Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase. Wahl, S., Barth, H., Ciossek, T., Aktories, K., Mueller, B.K. J. Cell Biol. (2000) [Pubmed]
  16. Sphingosine 1-phosphate stimulates fibronectin matrix assembly through a Rho-dependent signal pathway. Zhang, Q., Peyruchaud, O., French, K.J., Magnusson, M.K., Mosher, D.F. Blood (1999) [Pubmed]
  17. Alendronate inhibits lysophosphatidic acid-induced migration of human ovarian cancer cells by attenuating the activation of rho. Sawada, K., Morishige, K., Tahara, M., Kawagishi, R., Ikebuchi, Y., Tasaka, K., Murata, Y. Cancer Res. (2002) [Pubmed]
  18. ADP-ribosylation factor and Rho proteins mediate fMLP-dependent activation of phospholipase D in human neutrophils. Fensome, A., Whatmore, J., Morgan, C., Jones, D., Cockcroft, S. J. Biol. Chem. (1998) [Pubmed]
  19. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Gasman, S., Kalaidzidis, Y., Zerial, M. Nat. Cell Biol. (2003) [Pubmed]
  20. Assignment of the human RhoHP1 gene (ARHD) to chromosome 11q14.3 by radiation hybrid mapping. Kim, H.S., Choi, J.Y., Jung, A.R., Jang, K.L., Lee, W.H., Choi, W.C., Crow, T.J., Hyun, B.H. Cytogenet. Cell Genet. (2000) [Pubmed]
  21. Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Rittinger, K., Walker, P.A., Eccleston, J.F., Smerdon, S.J., Gamblin, S.J. Nature (1997) [Pubmed]
  22. Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein. Abdul-Manan, N., Aghazadeh, B., Liu, G.A., Majumdar, A., Ouerfelli, O., Siminovitch, K.A., Rosen, M.K. Nature (1999) [Pubmed]
  23. Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Fiorentini, C., Boquet, P. Nature (1997) [Pubmed]
  24. Focal adhesions, contractility, and signaling. Burridge, K., Chrzanowska-Wodnicka, M. Annu. Rev. Cell Dev. Biol. (1996) [Pubmed]
  25. G protein control of microtubule assembly. Zheng, Y. Annu. Rev. Cell Dev. Biol. (2004) [Pubmed]
  26. Regulation of receptor-mediated endocytosis by Rho and Rac. Lamaze, C., Chuang, T.H., Terlecky, L.J., Bokoch, G.M., Schmid, S.L. Nature (1996) [Pubmed]
  27. RanGAP mediates GTP hydrolysis without an arginine finger. Seewald, M.J., Körner, C., Wittinghofer, A., Vetter, I.R. Nature (2002) [Pubmed]
  28. C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Gosser, Y.Q., Nomanbhoy, T.K., Aghazadeh, B., Manor, D., Combs, C., Cerione, R.A., Rosen, M.K. Nature (1997) [Pubmed]
  29. Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. Zanata, S.M., Hovatta, I., Rohm, B., Püschel, A.W. J. Neurosci. (2002) [Pubmed]
  30. Rho proteins: linking signaling with membrane trafficking. Ridley, A.J. Traffic (2001) [Pubmed]
  31. The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Maesaki, R., Ihara, K., Shimizu, T., Kuroda, S., Kaibuchi, K., Hakoshima, T. Mol. Cell (1999) [Pubmed]
  32. Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. Takahashi, M., Mukai, H., Toshimori, M., Miyamoto, M., Ono, Y. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  33. The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Fuchs, U., Rehkamp, G., Haas, O.A., Slany, R., Kōnig, M., Bojesen, S., Bohle, R.M., Damm-Welk, C., Ludwig, W.D., Harbott, J., Borkhardt, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  34. Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation. Burns, S., Thrasher, A.J., Blundell, M.P., Machesky, L., Jones, G.E. Blood (2001) [Pubmed]
  35. Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE). Persidsky, Y., Heilman, D., Haorah, J., Zelivyanskaya, M., Persidsky, R., Weber, G.A., Shimokawa, H., Kaibuchi, K., Ikezu, T. Blood (2006) [Pubmed]
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