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Gene Review

RAB9A  -  RAB9A, member RAS oncogene family

Homo sapiens

Synonyms: RAB9, Ras-related protein Rab-9A
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Disease relevance of RAB9A


High impact information on RAB9A

  • A functional Rab9 binding site was required for TIP47 stimulation of MPR transport in vivo [5].
  • Our results demonstrate a role for Rab7 and Rab9 in the Golgi targeting of glycosphingolipids and suggest a new therapeutic approach for restoring normal lipid trafficking in NP-C cells [6].
  • These data provide the first indication that Rab9-mediated endosome to trans-Golgi transport can use a vesicle (rather than a tubular) intermediate [7].
  • Cation-independent mannose 6-phosphate receptors are enriched in the Rab9 domain relative to the Rab7 domain [7].
  • Rab9-positive transport vesicles fuse with the trans-Golgi network as followed by video microscopy of live cells [7].

Biological context of RAB9A

  • The Rab9 structure at near atomic resolution provides an excellent model for structure-based antiviral drug design [1].
  • Structure-based sequence alignment of Rab9 with other Rab proteins reveals that its active site consists of residues highly conserved in the Rab GTPase family, implying a common catalytic mechanism [1].
  • This effect is Rab9-specific since expression of Rab9 in untransformed NPC1 cells also leads to a reversal of their disease phenotype [8].
  • Here we report that ectopic expression of human telomerase reverse transcriptase (hTeRT) in human cells leads to an upregulation of the small GTPase Rab9 and its effector p40 [8].
  • During isolation and characterization of these cDNAs a Rab9 pseudogene was identified [2].

Anatomical context of RAB9A

  • Rab9 GTPase is required for the transport of mannose 6-phosphate receptors from endosomes to the trans-Golgi network in living cells, and in an in vitro system that reconstitutes this process [9].
  • These data are consistent with a model in which p40 and Rab9 act together to drive the process of transport vesicle docking [9].
  • Rab9 GTPase regulates late endosome size and requires effector interaction for its stability [10].
  • Moreover, Rab9 and the proteins with which it interacts seem critical for the maintenance of specific late endocytic compartments and endosome/lysosome localization [10].
  • To explore the importance of Rab9 for microdomain establishment, we depleted the protein from cultured cells [10].

Associations of RAB9A with chemical compounds


Other interactions of RAB9A


Analytical, diagnostic and therapeutic context of RAB9A

  • The most impaired mutant was indistinguishable from wild-type TIP47 in its circular dichroism spectrum, and mutant proteins that showed decreased Rab9 binding retained full capacity to bind to MPR cytoplasmic domains [16].
  • Moreover, co-immunoprecipitation experiments showed that Hook1 physically interacts with endocytic Rab7, Rab9 and Rab11, hence delineating a manifold role for mammalian Hook1 in membrane trafficking events [17].
  • Double-label immunofluorescence microscopy and subcellular fractionation studies indicated that NPC1 associates predominantly with late endosomes (Rab9 GTPase-positive vesicles) and, to a lesser extent, with lysosomes and the trans-Golgi network [18].


  1. High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target. Chen, L., DiGiammarino, E., Zhou, X.E., Wang, Y., Toh, D., Hodge, T.W., Meehan, E.J. J. Biol. Chem. (2004) [Pubmed]
  2. Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene. Davies, J.P., Cotter, P.D., Ioannou, Y.A. Genomics (1997) [Pubmed]
  3. Rab9 GTPase is required for replication of human immunodeficiency virus type 1, filoviruses, and measles virus. Murray, J.L., Mavrakis, M., McDonald, N.J., Yilla, M., Sheng, J., Bellini, W.J., Zhao, L., Le Doux, J.M., Shaw, M.W., Luo, C.C., Lippincott-Schwartz, J., Sanchez, A., Rubin, D.H., Hodge, T.W. J. Virol. (2005) [Pubmed]
  4. Protein transduction of Rab9 in Niemann-Pick C cells reduces cholesterol storage. Narita, K., Choudhury, A., Dobrenis, K., Sharma, D.K., Holicky, E.L., Marks, D.L., Walkley, S.U., Pagano, R.E. FASEB J. (2005) [Pubmed]
  5. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Carroll, K.S., Hanna, J., Simon, I., Krise, J., Barbero, P., Pfeffer, S.R. Science (2001) [Pubmed]
  6. Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells. Choudhury, A., Dominguez, M., Puri, V., Sharma, D.K., Narita, K., Wheatley, C.L., Marks, D.L., Pagano, R.E. J. Clin. Invest. (2002) [Pubmed]
  7. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. Barbero, P., Bittova, L., Pfeffer, S.R. J. Cell Biol. (2002) [Pubmed]
  8. Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes. Walter, M., Davies, J.P., Ioannou, Y.A. J. Lipid Res. (2003) [Pubmed]
  9. A novel Rab9 effector required for endosome-to-TGN transport. Díaz, E., Schimmöller, F., Pfeffer, S.R. J. Cell Biol. (1997) [Pubmed]
  10. Rab9 GTPase regulates late endosome size and requires effector interaction for its stability. Ganley, I.G., Carroll, K., Bittova, L., Pfeffer, S. Mol. Biol. Cell (2004) [Pubmed]
  11. Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides. Shapiro, A.D., Pfeffer, S.R. J. Biol. Chem. (1995) [Pubmed]
  12. Rab GDI: a solubilizing and recycling factor for rab9 protein. Soldati, T., Riederer, M.A., Pfeffer, S.R. Mol. Biol. Cell (1993) [Pubmed]
  13. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. Young, A.R., Chan, E.Y., Hu, X.W., Köchl, R., Crawshaw, S.G., High, S., Hailey, D.W., Lippincott-Schwartz, J., Tooze, S.A. J. Cell. Sci. (2006) [Pubmed]
  14. Small GTP-binding proteins in human endothelial cells. de Leeuw, H.P., Koster, P.M., Calafat, J., Janssen, H., van Zonneveld, A.J., van Mourik, J.A., Voorberg, J. Br. J. Haematol. (1998) [Pubmed]
  15. Active PIKfyve associates with and promotes the membrane attachment of the late endosome-to-trans-Golgi network transport factor Rab9 effector p40. Ikonomov, O.C., Sbrissa, D., Mlak, K., Deeb, R., Fligger, J., Soans, A., Finley, R.L., Shisheva, A. J. Biol. Chem. (2003) [Pubmed]
  16. Identification of residues in TIP47 essential for Rab9 binding. Hanna, J., Carroll, K., Pfeffer, S.R. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  17. Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway. Luiro, K., Yliannala, K., Ahtiainen, L., Maunu, H., Järvelä, I., Kyttälä, A., Jalanko, A. Hum. Mol. Genet. (2004) [Pubmed]
  18. Niemann-Pick C1 is a late endosome-resident protein that transiently associates with lysosomes and the trans-Golgi network. Higgins, M.E., Davies, J.P., Chen, F.W., Ioannou, Y.A. Mol. Genet. Metab. (1999) [Pubmed]
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