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Gene Review

RAB15  -  RAB15, member RAS oncogene family

Homo sapiens

Synonyms: Ras-related protein Rab-15
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High impact information on RAB15

  • We previously reported that Rab15 differentially regulates transferrin receptor trafficking through sorting endosomes and the endocytic recycling compartment, suggesting a role for distinct Rab15-effector interactions at these endocytic compartments [1].
  • Rab15 may interfere with Rab5 function directly by sequestering Rab5 effectors or indirectly through novel sets of effector interactions [2].
  • Mammalian suppressor of Sec4 modulates the inhibitory effect of Rab15 during early endocytosis [2].
  • Mutational analysis of Rab15 indicates that lysine at position 48 (K48Q) is important for the binding of Rab15-GDP to Mss4 [2].
  • Moreover, the mutation K48Q counters the inhibitory phenotype of wild type Rab15 on receptor-mediated endocytosis in HeLa cells and homotypic endosome fusion in vitro without altering the relative amount of cell surface-associated transferrin receptor [2].

Anatomical context of RAB15

  • This data suggests that rab15 may act in concert with rab3A in regulating aspects of synaptic vesicle membrane flow within the nerve terminal [3].
  • We recently demonstrated that epitope-tagged Rab15 (HArab15) co-localizes with Rab4, -5, and -11 on early endosomal membranes in CHO cells (Zuk, P. A., and Elferink, L. A. (1999) J. Biol. Chem. 274, 22303-22312) [4].


  1. Rab15 effector protein: a novel protein for receptor recycling from the endocytic recycling compartment. Strick, D.J., Elferink, L.A. Mol. Biol. Cell (2005) [Pubmed]
  2. Mammalian suppressor of Sec4 modulates the inhibitory effect of Rab15 during early endocytosis. Strick, D.J., Francescutti, D.M., Zhao, Y., Elferink, L.A. J. Biol. Chem. (2002) [Pubmed]
  3. rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain. Elferink, L.A., Anzai, K., Scheller, R.H. J. Biol. Chem. (1992) [Pubmed]
  4. Rab15 differentially regulates early endocytic trafficking. Zuk, P.A., Elferink, L.A. J. Biol. Chem. (2000) [Pubmed]
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