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Gene Review

Rab43  -  RAB43, member RAS oncogene family

Mus musculus

Synonyms: 1810048P08Rik, 2500004H21Rik, AW490415, Ras-related protein Rab-43
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Disease relevance of Rab43

  • Rab GGTase inhibition may represent a new treatment for thrombocytosis and clotting disorders [1].
  • Live Salmonella modulate expression of Rab proteins to persist in a specialized compartment and escape transport to lysosomes [2].
  • Second, the position of the nitrogen in the side chain of phosphonocarboxylates is crucial for their ability to inhibit Rab prenylation and hence to inhibit bone resorption [3].
  • Since proteins belonging to the Rab family have already been related to retinal degeneration we considered RAB23 an interesting candidate for the RP25 locus [4].

High impact information on Rab43

  • The Rab family of low-molecular-mass GTP-binding proteins are thought to guide membrane fusion between a transport vesicle and the target membrane, and to determine the specificity of docking [5].
  • In brain, the Rab protein Rab3A is specific to synaptic vesicles, whose exocytosis can be monitored with submillisecond resolution by following synaptic transmission [5].
  • The Rab GTPase effector Noc2 was brought into the limelight by a recent publication that demonstrated its requirements at different stages of regulated exocytosis [6].
  • REP1 is involved in lipid modification (prenylation) of Rab GTPases, key regulators of intracellular vesicular transport and organelle dynamics [7].
  • Heterozygous-null females exhibit characteristic hallmarks of CHM: progressive degeneration of the photoreceptors, patchy depigmentation of the RPE, and Rab prenylation defects [7].

Biological context of Rab43

  • This work identifies a key role for the Rab38/Rab32 subfamily of Rab proteins in the biogenesis of melanosomes and potentially other lysosome-related organelles [8].
  • Our data provide the first evidence for a dual role of a Rab GTPase in regulating both generation and turnover of PIs via PI kinases and phosphatases to coordinate signaling functions with organelle homeostasis [9].
  • Screening its possible Rab partner by a yeast two-hybrid system revealed that an amino-terminal zinc-finger domain of granuphilin interacts with Rab27a [10].
  • These Rab proteins regulate the endocytosis and recycling or degradation of activated receptor tyrosine kinases such as the platelet-derived growth factor receptor (PDGFR) [11].
  • Rabphilin is a membrane trafficking protein on secretory vesicles that consists of an N-terminal Rab-binding domain and C-terminal tandem C2 domains [12].

Anatomical context of Rab43

  • These results provide the first molecular description of an organelle receptor for an actin-based motor, illustrate how alternate exon usage can be used to specify cargo, and further expand the functional repertoire of Rab GTPases and their effectors [13].
  • Rab GTPases are regulators of intracellular membrane traffic [14].
  • The association of Rab27b with fusiform vesicles and its differentiation-dependent expression suggest that this Rab protein plays a role in regulating the delivery of fusiform vesicles to the apical plasma membrane of umbrella cells [15].
  • Rab function is regulated by GDP dissociation inhibitor (GDI), which releases Rab proteins from membranes and inhibits GDP dissociation [16].
  • A novel set of Rab and its effector, Rab27a/granuphilin, which is localized on insulin granules in pancreatic beta cells, was recently identified [17].

Associations of Rab43 with chemical compounds

  • Guanine nucleotide exchange is essential for Rab GTPase activities in regulating intracellular vesicle trafficking [18].
  • The importance of the Rab family of small GTPases (guanosine 5'-triphosphatases) in platelet biogenesis is revealed in gunmetal (gm/gm) mice, which show deficient Rab isoprenylation and macrothrombocytopenia with few granules and abnormal megakaryocyte morphology [19].
  • Rab proteins typically lack the consensus carboxyl-terminal CXXX motif that signals isoprenoid modification of Ras and other isoprenylated proteins and, instead, terminate in either CC or CXC sequences (C = cysteine, X = any amino acid) [20].
  • Contrary to the cytosolic localization of all known GDI proteins, acting on Rab or Rho, RhoGDI-3 is associated to a Triton X-100-insoluble membranous or cytoskeletal subcellular fraction [21].
  • Our results suggest that homotypic fusion of ER membranes requires Rab and that Rab activation is a transient event necessary for the formation of a fusion pore leading to the mixing of luminal contents of ER microsomes [22].

Analytical, diagnostic and therapeutic context of Rab43

  • We report here the molecular cloning and characterization of a novel Rab protein, Rab33B [23].
  • The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach [24].
  • To localize Rab GDI, we processed cells from different sources for indirect immunofluorescence microscopy [25].


  1. Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis. Detter, J.C., Zhang, Q., Mules, E.H., Novak, E.K., Mishra, V.S., Li, W., McMurtrie, E.B., Tchernev, V.T., Wallace, M.R., Seabra, M.C., Swank, R.T., Kingsmore, S.F. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. Live Salmonella modulate expression of Rab proteins to persist in a specialized compartment and escape transport to lysosomes. Hashim, S., Mukherjee, K., Raje, M., Basu, S.K., Mukhopadhyay, A. J. Biol. Chem. (2000) [Pubmed]
  3. Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo. Coxon, F.P., Ebetino, F.H., Mules, E.H., Seabra, M.C., McKenna, C.E., Rogers, M.J. Bone (2005) [Pubmed]
  4. Molecular cloning and characterization of human RAB23, a member of the group of Rab GTPases. Marcos, I., Borrego, S., Antiñolo, G. Int. J. Mol. Med. (2003) [Pubmed]
  5. The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Geppert, M., Goda, Y., Stevens, C.F., Südhof, T.C. Nature (1997) [Pubmed]
  6. Noc-king out exocrine and endocrine secretion. Cheviet, S., Waselle, L., Regazzi, R. Trends Cell Biol. (2004) [Pubmed]
  7. Independent degeneration of photoreceptors and retinal pigment epithelium in conditional knockout mouse models of choroideremia. Tolmachova, T., Anders, R., Abrink, M., Bugeon, L., Dallman, M.J., Futter, C.E., Ramalho, J.S., Tonagel, F., Tanimoto, N., Seeliger, M.W., Huxley, C., Seabra, M.C. J. Clin. Invest. (2006) [Pubmed]
  8. Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes. Wasmeier, C., Romao, M., Plowright, L., Bennett, D.C., Raposo, G., Seabra, M.C. J. Cell Biol. (2006) [Pubmed]
  9. An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway. Shin, H.W., Hayashi, M., Christoforidis, S., Lacas-Gervais, S., Hoepfner, S., Wenk, M.R., Modregger, J., Uttenweiler-Joseph, S., Wilm, M., Nystuen, A., Frankel, W.N., Solimena, M., De Camilli, P., Zerial, M. J. Cell Biol. (2005) [Pubmed]
  10. The Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granules. Yi, Z., Yokota, H., Torii, S., Aoki, T., Hosaka, M., Zhao, S., Takata, K., Takeuchi, T., Izumi, T. Mol. Cell. Biol. (2002) [Pubmed]
  11. The p85alpha subunit of phosphatidylinositol 3'-kinase binds to and stimulates the GTPase activity of Rab proteins. Chamberlain, M.D., Berry, T.R., Pastor, M.C., Anderson, D.H. J. Biol. Chem. (2004) [Pubmed]
  12. The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. Tsuboi, T., Fukuda, M. J. Biol. Chem. (2005) [Pubmed]
  13. Identification of an organelle receptor for myosin-Va. Wu, X.S., Rao, K., Zhang, H., Wang, F., Sellers, J.R., Matesic, L.E., Copeland, N.G., Jenkins, N.A., Hammer, J.A. Nat. Cell Biol. (2002) [Pubmed]
  14. Rab27a regulates the peripheral distribution of melanosomes in melanocytes. Hume, A.N., Collinson, L.M., Rapak, A., Gomes, A.Q., Hopkins, C.R., Seabra, M.C. J. Cell Biol. (2001) [Pubmed]
  15. Rab27b is associated with fusiform vesicles and may be involved in targeting uroplakins to urothelial apical membranes. Chen, Y., Guo, X., Deng, F.M., Liang, F.X., Sun, W., Ren, M., Izumi, T., Sabatini, D.D., Sun, T.T., Kreibich, G. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  16. Cloning, characterization, and expression of a novel GDP dissociation inhibitor isoform from skeletal muscle. Shisheva, A., Südhof, T.C., Czech, M.P. Mol. Cell. Biol. (1994) [Pubmed]
  17. Granuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1a. Torii, S., Zhao, S., Yi, Z., Takeuchi, T., Izumi, T. Mol. Cell. Biol. (2002) [Pubmed]
  18. The Rab3 GDP/GTP exchange factor homolog AEX-3 has a dual function in synaptic transmission. Iwasaki, K., Toyonaga, R. EMBO J. (2000) [Pubmed]
  19. A role for Rab27b in NF-E2-dependent pathways of platelet formation. Tiwari, S., Italiano, J.E., Barral, D.C., Mules, E.H., Novak, E.K., Swank, R.T., Seabra, M.C., Shivdasani, R.A. Blood (2003) [Pubmed]
  20. Ras (CXXX) and Rab (CC/CXC) prenylation signal sequences are unique and functionally distinct. Khosravi-Far, R., Clark, G.J., Abe, K., Cox, A.D., McLain, T., Lutz, R.J., Sinensky, M., Der, C.J. J. Biol. Chem. (1992) [Pubmed]
  21. RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG. Zalcman, G., Closson, V., Camonis, J., Honoré, N., Rousseau-Merck, M.F., Tavitian, A., Olofsson, B. J. Biol. Chem. (1996) [Pubmed]
  22. A Rab GTPase is required for homotypic assembly of the endoplasmic reticulum. Turner, M.D., Plutner, H., Balch, W.E. J. Biol. Chem. (1997) [Pubmed]
  23. A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae. Zheng, J.Y., Koda, T., Fujiwara, T., Kishi, M., Ikehara, Y., Kakinuma, M. J. Cell. Sci. (1998) [Pubmed]
  24. The complexity of the Rab and Rho GTP-binding protein subfamilies revealed by a PCR cloning approach. Chavrier, P., Simons, K., Zerial, M. Gene (1992) [Pubmed]
  25. Production and characterization of isotype-specific monoclonal antibodies to bovine brain Rab GDI. Ha, S.G., Park, J.B., Ko, K.H., Choi, E.Y. Hybridoma (1999) [Pubmed]
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