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Gene Review

RAB1A  -  RAB1A, member RAS oncogene family

Homo sapiens

Synonyms: RAB1, Ras-related protein Rab-1A, YPT1, YPT1-related protein
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Disease relevance of RAB1A

  • Aberrant expression of RAB1A in human tongue cancer [1].
  • We show that rab1 is an excellent marker of the intermediate compartment, and we use this marker, as well as budding profiles of the mouse hepatitis virus (MHV) in cells infected with this virus, to identify this compartment [2].
  • The cells were also tested for the FMC7, defined previously on PLL cells and the RAB1, a newly described hairy cell leukemia antigen [3].
  • These results indicate that increased expression of Rab1 GTPase in myocardium distorts subcellular localization of proteins and is sufficient to cause cardiac hypertrophy and failure [4].

High impact information on RAB1A

  • We identify protein partners for TIR-1 and show that the small GTPase Rab1 and the f subunit of ATP synthase participate specifically in the control of antimicrobial peptide gene expression [5].
  • Golgin-84 binds to active rab1 but not cis-Golgi matrix proteins [6].
  • A GDP-bound of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments [7].
  • The mutant protein required posttranslational isoprenylation for inhibition and behaved as a competitive inhibitor of wild-type rab1 function [7].
  • Hydroxymethylglutaryl-CoA reductase, the key enzyme of cholesterol biosynthesis, colocalized with slowly sedimenting, Rab1-enriched membranes when the IC subdomains were separated by velocity sedimentation [8].

Biological context of RAB1A


Anatomical context of RAB1A


Associations of RAB1A with chemical compounds

  • Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step [16].
  • Regulation of the cell surface expression and function of angiotensin II type 1 receptor by Rab1-mediated endoplasmic reticulum-to-Golgi transport in cardiac myocytes [17].
  • Brefeldin A inhibited beta-AR and alpha1-AR export and antagonized the Rab1 effect on alpha1-AR expression [18].
  • Consistent with the effects on receptor cell-surface targeting, Rab1 selectively enhanced ERK1/2 activation and hypertrophic growth in response to the alpha1-AR agonist phenylephrine but not to the beta-AR agonist isoproterenol [18].
  • SidM is a guanosine nucleotide exchange factor for Rab1 that recruits Rab1 to Legionella-containing vacuoles, a process that is enhanced by LidA [19].

Regulatory relationships of RAB1A

  • These data indicate that Rab1 GTPase selectively regulates intracellular trafficking and signaling of G protein-coupled receptors and suggest a novel, as yet undefined pathway for movement of G protein-coupled receptors from the ER to the cell surface [10].

Other interactions of RAB1A

  • MICAL-1 isoforms, novel rab1 interacting proteins [13].
  • The rab1, rab2, rab3A, and rab4 proteins are the human counterparts of the rat rab gene products that we have previously characterized [20].
  • Cell fractionation revealed that in contrast to the mainly membrane-associated rab1 effector GM130, MICAL-1 displays a predominantly cytosolic localization [13].
  • A similar binding was seen to rab1 but not to rab6, both Golgi rabs [21].
  • RESULTS: Here, we report the characterization of Iporin, which is similar to KIAA0375 as a novel rab1-interacting protein [14].

Analytical, diagnostic and therapeutic context of RAB1A


  1. Aberrant expression of RAB1A in human tongue cancer. Shimada, K., Uzawa, K., Kato, M., Endo, Y., Shiiba, M., Bukawa, H., Yokoe, H., Seki, N., Tanzawa, H. Br. J. Cancer (2005) [Pubmed]
  2. Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. Griffiths, G., Ericsson, M., Krijnse-Locker, J., Nilsson, T., Goud, B., Söling, H.D., Tang, B.L., Wong, S.H., Hong, W. J. Cell Biol. (1994) [Pubmed]
  3. Further characterization of prolymphocytic leukemia cells as a tumor of activated B cells. Berrebi, A., Bassous-Guedj, L., Vorst, E., Dagan, S., Shtalrid, M., Freedman, A. Am. J. Hematol. (1990) [Pubmed]
  4. Increased myocardial Rab GTPase expression: a consequence and cause of cardiomyopathy. Wu, G., Yussman, M.G., Barrett, T.J., Hahn, H.S., Osinska, H., Hilliard, G.M., Wang, X., Toyokawa, T., Yatani, A., Lynch, R.A., Robbins, J., Dorn, G.W. Circ. Res. (2001) [Pubmed]
  5. TLR-independent control of innate immunity in Caenorhabditis elegans by the TIR domain adaptor protein TIR-1, an ortholog of human SARM. Couillault, C., Pujol, N., Reboul, J., Sabatier, L., Guichou, J.F., Kohara, Y., Ewbank, J.J. Nat. Immunol. (2004) [Pubmed]
  6. The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. Diao, A., Rahman, D., Pappin, D.J., Lucocq, J., Lowe, M. J. Cell Biol. (2003) [Pubmed]
  7. A GDP-bound of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments. Nuoffer, C., Davidson, H.W., Matteson, J., Meinkoth, J., Balch, W.E. J. Cell Biol. (1994) [Pubmed]
  8. Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Sannerud, R., Marie, M., Nizak, C., Dale, H.A., Pernet-Gallay, K., Perez, F., Goud, B., Saraste, J. Mol. Biol. Cell (2006) [Pubmed]
  9. YAC contigs of the Rab1 and wobbler (wr) spinal muscular atrophy gene region on proximal mouse chromosome 11 and of the homologous region on human chromosome 2p. Wedemeyer, N., Lengeling, A., Ronsiek, M., Korthaus, D., Baer, K., Wuttke, M., Jockusch, H. Genomics (1996) [Pubmed]
  10. Distinct pathways for the trafficking of angiotensin II and adrenergic receptors from the endoplasmic reticulum to the cell surface: Rab1-independent transport of a G protein-coupled receptor. Wu, G., Zhao, G., He, Y. J. Biol. Chem. (2003) [Pubmed]
  11. rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif. Kinsella, B.T., Maltese, W.A. J. Biol. Chem. (1991) [Pubmed]
  12. Nucleotide sequence of a new YPT1-related human cDNA which belongs to the ras gene superfamily. Tachibana, K., Umezawa, A., Kato, S., Takano, T. Nucleic Acids Res. (1988) [Pubmed]
  13. MICAL-1 isoforms, novel rab1 interacting proteins. Weide, T., Teuber, J., Bayer, M., Barnekow, A. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  14. Identification and characterization of Iporin as a novel interaction partner for rab1. Bayer, M., Fischer, J., Kremerskothen, J., Ossendorf, E., Matanis, T., Konczal, M., Weide, T., Barnekow, A. BMC Cell Biol. (2005) [Pubmed]
  15. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. Tisdale, E.J., Bourne, J.R., Khosravi-Far, R., Der, C.J., Balch, W.E. J. Cell Biol. (1992) [Pubmed]
  16. Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step. Peter, F., Wong, S.H., Subramaniam, V.N., Tang, B.L., Hong, W. J. Cell. Sci. (1998) [Pubmed]
  17. Regulation of the cell surface expression and function of angiotensin II type 1 receptor by Rab1-mediated endoplasmic reticulum-to-Golgi transport in cardiac myocytes. Filipeanu, C.M., Zhou, F., Claycomb, W.C., Wu, G. J. Biol. Chem. (2004) [Pubmed]
  18. Differential regulation of the cell-surface targeting and function of beta- and alpha1-adrenergic receptors by Rab1 GTPase in cardiac myocytes. Filipeanu, C.M., Zhou, F., Fugetta, E.K., Wu, G. Mol. Pharmacol. (2006) [Pubmed]
  19. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Machner, M.P., Isberg, R.R. Dev. Cell (2006) [Pubmed]
  20. The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. Zahraoui, A., Touchot, N., Chardin, P., Tavitian, A. J. Biol. Chem. (1989) [Pubmed]
  21. Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. Valsdottir, R., Hashimoto, H., Ashman, K., Koda, T., Storrie, B., Nilsson, T. FEBS Lett. (2001) [Pubmed]
  22. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Cooper, A.A., Gitler, A.D., Cashikar, A., Haynes, C.M., Hill, K.J., Bhullar, B., Liu, K., Xu, K., Strathearn, K.E., Liu, F., Cao, S., Caldwell, K.A., Caldwell, G.A., Marsischky, G., Kolodner, R.D., Labaer, J., Rochet, J.C., Bonini, N.M., Lindquist, S. Science (2006) [Pubmed]
  23. RAB-1: a new monoclonal antibody to leukemic hairy cells. Berrebi, A., Eshhar, Z., Linder, S., Guedj, L., Avraham, H. Leuk. Res. (1986) [Pubmed]
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