The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RPH3A  -  rabphilin 3A

Homo sapiens

Synonyms: Exophilin-1, KIAA0985, Rabphilin-3A, exophilin-1, rabphilin
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of RPH3A


High impact information on RPH3A

  • The core secondary structures are similar to a rabphilin-3A Zn2+-binding domain and to the C1 and LIM domains [3].
  • It is proposed to form a novel interface for a Rab11 partner compatible with the simultaneous binding of another partner at the Rabphilin interface [4].
  • Therefore, the Rab3-GAP-binding site involves the switch I region of Rab3 and overlaps with the Rabphilin-binding domain [5].
  • The membrane association of rabphilin-3A was modestly enhanced in Rab3B-expressing PC12 cells relative to Rab3A-overexpressing cells [6].
  • Overexpression of wild-type Rabphilin in the insulin-secreting cell line HIT-T15 did not affect receptor-mediated transferrin endocytosis [7].

Biological context of RPH3A


Anatomical context of RPH3A


Associations of RPH3A with chemical compounds

  • Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine [8].
  • These results indicate that Rabphilin-3A binds to a protein molecule with a M(r) of 115 kDa through the C2 domain in the presence of phosphatidylserine and Ca2+ [15].
  • To identify a Rabphilin-3A-interacting protein, proteins were immunoprecipitated by an anti-Rabphilin-3A polyclonal antibody from the lysate of PC12 cells and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by protein staining [16].
  • In this study we demonstrated by a mutation analysis that the polybasic sequence (587 KKAKHKTQIKKK 598) in the C2B domain of rabphilin is required for SNAP-25 binding, and that the Asp residues in the Ca(2+)-binding loop 3 (D628 and D630) of the C2B domain are not required [17].
  • Accordingly, significant modification of the secretory responses was observed, at the cell population level, upon transient expression of the serotonin transporter and of proteins known to interfere with exocytosis, such as botulinum neurotoxin C1, GTPase-deficient Rab3 proteins, truncated Rabphilin constructs or Rim [18].

Physical interactions of RPH3A


Regulatory relationships of RPH3A


Other interactions of RPH3A


Analytical, diagnostic and therapeutic context of RPH3A


  1. Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease. Dalfó, E., Barrachina, M., Rosa, J.L., Ambrosio, S., Ferrer, I. Neurobiol. Dis. (2004) [Pubmed]
  2. Exophilin A, a new antibiotic from a marine microorganism Exophiala pisciphila. Doshida, J., Hasegawa, H., Onuki, H., Shimidzu, N. J. Antibiot. (1996) [Pubmed]
  3. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Misra, S., Hurley, J.H. Cell (1999) [Pubmed]
  4. The structural GDP/GTP cycle of Rab11 reveals a novel interface involved in the dynamics of recycling endosomes. Pasqualato, S., Senic-Matuglia, F., Renault, L., Goud, B., Salamero, J., Cherfils, J. J. Biol. Chem. (2004) [Pubmed]
  5. Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP. Clabecq, A., Henry, J.P., Darchen, F. J. Biol. Chem. (2000) [Pubmed]
  6. Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells. Weber, E., Jilling, T., Kirk, K.L. J. Biol. Chem. (1996) [Pubmed]
  7. 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]
  8. Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine. Miyazaki, M., Shirataki, H., Kohno, H., Kaibuchi, K., Tsugita, A., Takai, Y. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  9. Characterization of rabphilin phosphorylation using phospho-specific antibodies. Lonart, G., Südhof, T.C. Neuropharmacology (2001) [Pubmed]
  10. The stimulatory effect of rabphilin 3a on regulated exocytosis from insulin-secreting cells does not require an association-dissociation cycle with membranes mediated by Rab 3. Arribas, M., Regazzi, R., Garcia, E., Wollheim, C.B., De Camilli, P. Eur. J. Cell Biol. (1997) [Pubmed]
  11. Rabphilin-3A: a multifunctional regulator of synaptic vesicle traffic. Burns, M.E., Sasaki, T., Takai, Y., Augustine, G.J. J. Gen. Physiol. (1998) [Pubmed]
  12. Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin. Perin, M.S. Biochemistry (1996) [Pubmed]
  13. Cloning of a mouse Rabphilin-3A expressed in hormone-secreting cells. Inagaki, N., Mizuta, M., Seino, S. J. Biochem. (1994) [Pubmed]
  14. Expression, localization and functional role of small GTPases of the Rab3 family in insulin-secreting cells. Regazzi, R., Ravazzola, M., Iezzi, M., Lang, J., Zahraoui, A., Andereggen, E., Morel, P., Takai, Y., Wollheim, C.B. J. Cell. Sci. (1996) [Pubmed]
  15. Rabphilin-3A binds to a M(r) 115,000 polypeptide in a phosphatidylserine- and Ca(2+)-dependent manner. Miyazaki, M., Kaibuchi, K., Shirataki, H., Kohno, H., Ueyama, T., Nishikawa, J., Takai, Y. Brain Res. Mol. Brain Res. (1995) [Pubmed]
  16. Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells. Imazumi, K., Sasaki, T., Takahashi, K., Takai, Y. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  17. The polybasic sequence in the C2B domain of rabphilin is required for the vesicle docking step in PC12 cells. Tsuboi, T., Kanno, E., Fukuda, M. J. Neurochem. (2007) [Pubmed]
  18. Transmitter uptake and release in PC12 cells overexpressing plasma membrane monoamine transporters. Schonn, J.S., Desnos, C., Henry, J.P., Darchen, F. J. Neurochem. (2003) [Pubmed]
  19. GDP/GTP exchange reaction-stimulating activity of Rabphilin-3A for Rab3A small GTP-binding protein. Fujita, Y., Sasaki, T., Araki, K., Takahashi, K., Imazumi, K., Kato, M., Matsuura, Y., Takai, Y. FEBS Lett. (1994) [Pubmed]
  20. Myosin-V, a versatile motor for short-range vesicle transport. Langford, G.M. Traffic (2002) [Pubmed]
  21. Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27.effector complex. Fukuda, M. Biochem. Soc. Trans. (2006) [Pubmed]
WikiGenes - Universities