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Gene Review

RABEP1  -  rabaptin, RAB GTPase binding effector...

Homo sapiens

Synonyms: RAB5EP, RABPT5, RABPT5A, Rab GTPase-binding effector protein 1, Rabaptin-4, ...
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Disease relevance of RABEP1


High impact information on RABEP1


Biological context of RABEP1


Anatomical context of RABEP1

  • Collectively, our data show that rab4-GTP acts as a scaffold for a rabaptin-5alpha- gamma(1)-adaptin complex on recycling endosomes and that interactions between rab4, rabaptin-5alpha and gamma(1)-adaptin regulate membrane recycling [6].
  • Transduction with a retroviral vector expressing rabaptin-5/PDGFbetaR transformed the hematopoietic cell line Ba/F3 to growth factor independence and caused a fatal myeloproliferative disease in mice [1].
  • Modulation of endocytosis by GAP-43, in association with rabaptin-5, may constitute a common molecular mechanism by which GAP-43 regulates membrane dynamics during its known roles in activity-dependent neurotransmitter release and neurite outgrowth [8].
  • These results suggest that inactivation of Rabaptin-5 and inhibition of vesicle transport lead to fragmentation of endosomes and inhibition of the endocytic pathway during the execution phase of apoptosis [10].
  • Immunodepletion of the Rabaptin-5beta complex from cytosol only partially inhibits early endosome fusion in vitro, whereas the additional depletion of the Rabaptin-5 complex has a stronger inhibitory effect [11].

Associations of RABEP1 with chemical compounds

  • The new fusion protein includes more than 85% of the native Rabaptin-5 fused to the transmembrane and intracellular tyrosine kinase domains of the PDGFbetaR [1].
  • Immunocytochemical analysis showed that gamma1-adaptin and Rabaptin-5 colocalize to a significant extent on perinuclear structures, probably on recycling endosomes, and are redistributed into the cytoplasm upon treatment with brefeldin A [12].
  • GGAs possess four conserved functional domains, each of which interacts with cargo proteins including mannose 6-phosphate receptors, the small GTPase ARF, clathrin, or accessory proteins including Rabaptin-5 and gamma-synergin [13].

Physical interactions of RABEP1

  • The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis [8].
  • Rabaptin-5 also binds the active form of GTPase Rab5 [14].
  • Gamma-adaptin interacts directly with Rabaptin-5 through its ear domain [12].
  • We determined the structure of the GAE domain of human GGA3 in complex with a peptide based on the DFGPLV sequence of the accessory protein Rabaptin-5 and refined it at a resolution of 2.2 A [15].
  • In this study, we define the Rabaptin-5 binding site on the GGA1-GAT domain and its relationship to the binding sites for ubiquitin and TSG101 [16].

Regulatory relationships of RABEP1


Other interactions of RABEP1

  • A GST-rab33b fusion protein stabilised in its GTP form was found to interact by Western blotting or mass spectroscopy with Golgi protein GM130 and rabaptin-5 and rabex-5, two rab effector molecules thought to function exclusively in the endocytic pathway [18].
  • Our observations show that Rabaptin-5, ubiquitin, and TSG101 bind to overlapping but distinct binding sites on the trihelical bundle [16].
  • This process requires EEA1 in addition to the Rabaptin-5 complex [19].
  • The interaction of the human GGA1 GAT domain with rabaptin-5 is mediated by residues on its three-helix bundle [20].
  • Furthermore, a reversed mutation, S293N, in GGA3 partially establishes Rabaptin-5 binding ability in its GAT domain [20].

Analytical, diagnostic and therapeutic context of RABEP1


  1. Rabaptin-5 is a novel fusion partner to platelet-derived growth factor beta receptor in chronic myelomonocytic leukemia. Magnusson, M.K., Meade, K.E., Brown, K.E., Arthur, D.C., Krueger, L.A., Barrett, A.J., Dunbar, C.E. Blood (2001) [Pubmed]
  2. Endocytic pathway alterations in human hippocampus after global ischemia and the influence of APOE genotype. McColl, B.W., Graham, D.I., Weir, C.J., White, F., Horsburgh, K. Am. J. Pathol. (2003) [Pubmed]
  3. Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy. Nakamura, S., Kawamoto, Y., Nakano, S., Akiguchi, I. Clin. Neuropathol. (2000) [Pubmed]
  4. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Horiuchi, H., Lippé, R., McBride, H.M., Rubino, M., Woodman, P., Stenmark, H., Rybin, V., Wilm, M., Ashman, K., Mann, M., Zerial, M. Cell (1997) [Pubmed]
  5. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Stenmark, H., Vitale, G., Ullrich, O., Zerial, M. Cell (1995) [Pubmed]
  6. Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes. Deneka, M., Neeft, M., Popa, I., van Oort, M., Sprong, H., Oorschot, V., Klumperman, J., Schu, P., van der Sluijs, P. EMBO J. (2003) [Pubmed]
  7. Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5. Vitale, G., Rybin, V., Christoforidis, S., Thornqvist, P., McCaffrey, M., Stenmark, H., Zerial, M. EMBO J. (1998) [Pubmed]
  8. The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis. Neve, R.L., Coopersmith, R., McPhie, D.L., Santeufemio, C., Pratt, K.G., Murphy, C.J., Lynn, S.D. J. Neurosci. (1998) [Pubmed]
  9. Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis. Swanton, E., Bishop, N., Woodman, P. J. Biol. Chem. (1999) [Pubmed]
  10. Cleavage of rabaptin-5 blocks endosome fusion during apoptosis. Cosulich, S.C., Horiuchi, H., Zerial, M., Clarke, P.R., Woodman, P.G. EMBO J. (1997) [Pubmed]
  11. Two distinct effectors of the small GTPase Rab5 cooperate in endocytic membrane fusion. Gournier, H., Stenmark, H., Rybin, V., Lippé, R., Zerial, M. EMBO J. (1998) [Pubmed]
  12. Gamma-adaptin interacts directly with Rabaptin-5 through its ear domain. Shiba, Y., Takatsu, H., Shin, H.W., Nakayama, K. J. Biochem. (2002) [Pubmed]
  13. The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads. Nakayama, K., Wakatsuki, S. Cell Struct. Funct. (2003) [Pubmed]
  14. The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis. Xiao, G.H., Shoarinejad, F., Jin, F., Golemis, E.A., Yeung, R.S. J. Biol. Chem. (1997) [Pubmed]
  15. Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3. Miller, G.J., Mattera, R., Bonifacino, J.S., Hurley, J.H. Nat. Struct. Biol. (2003) [Pubmed]
  16. The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. Mattera, R., Puertollano, R., Smith, W.J., Bonifacino, J.S. J. Biol. Chem. (2004) [Pubmed]
  17. Rabphilin dissociated from Rab3 promotes endocytosis through interaction with Rabaptin-5. Coppola, T., Hirling, H., Perret-Menoud, V., Gattesco, S., Catsicas, S., Joberty, G., Macara, I.G., Regazzi, R. J. Cell. Sci. (2001) [Pubmed]
  18. 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]
  19. Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. Rubino, M., Miaczynska, M., Lippé, R., Zerial, M. J. Biol. Chem. (2000) [Pubmed]
  20. The interaction of the human GGA1 GAT domain with rabaptin-5 is mediated by residues on its three-helix bundle. Zhai, P., He, X., Liu, J., Wakeham, N., Zhu, G., Li, G., Tang, J., Zhang, X.C. Biochemistry (2003) [Pubmed]
  21. Multiple Rabaptin-5-like transcripts. Korobko, E.V., Kiselev, S.L., Korobko, I.V. Gene (2002) [Pubmed]
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