RAB18

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RAB18, member RAS oncogene family

PDB rendering based on 1x3s.
Identifiers
Symbols RAB18; RAB18LI1
External IDs OMIM602207 MGI102790 HomoloGene40765 GeneCards: RAB18 Gene
Orthologs
Species Human Mouse
Entrez 22931 19330
Ensembl ENSG00000099246 ENSMUSG00000073639
UniProt Q9NP72 Q0PD38
RefSeq (mRNA) NM_021252 NM_181070.5
RefSeq (protein) NP_067075 NP_851415.1
Location (UCSC) Chr 10:
27.79 – 27.83 Mb
Chr 18:
6.77 – 6.79 Mb
PubMed search [1] [2]

Ras-related protein Rab-18 is a protein that in humans is encoded by the RAB18 gene.[1][2]

Rab18 is a ubiquitously expressed protein with particularly high expression in brain and adipose tissue.[3] Rab18 was first characterised as an endosomal protein in epithelial cells of mouse kidney and intestines.[3] Subsequent studies revealed that Rab18 has a wide intracellular distribution; localising to the Golgi complex, endoplasmic reticulum, lipid droplets, and cytosol of various cell types.[4][5][6] In the brain, Rab18 has been isolated in association with synaptic vesicles[7][8] and has been observed to localise to secretory granules in neuroendocrine cells.[9]

[edit] References

  1. ^ Schafer U, Seibold S, Schneider A, Neugebauer E (Feb 2000). "Isolation and characterisation of the human rab18 gene after stimulation of endothelial cells with histamine". FEBS Lett 466 (1): 148–54. doi:10.1016/S0014-5793(99)01778-0. PMID 10648831. 
  2. ^ "Entrez Gene: RAB18 RAB18, member RAS oncogene family". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22931. 
  3. ^ a b Lütcke A, Parton RG, Murphy C, Olkkonen VM, Dupree P, Valencia A, Simons K, Zerial M (December 1994). "Cloning and subcellular localization of novel rab proteins reveals polarized and cell type-specific expression". J. Cell. Sci. 107 (12): 3437–48. PMID 7706395. 
  4. ^ Dejgaard SY, Murshid A, Erman A, Kizilay O, Verbich D, Lodge R, Dejgaard K, Ly-Hartig TB, Pepperkok R, Simpson JC, Presley JF (August 2008). "Rab18 and Rab43 have key roles in ER-Golgi trafficking". J. Cell. Sci. 121 (Pt 16): 2768–81. doi:10.1242/jcs.021808. PMID 18664496. 
  5. ^ Martin S, Driessen K, Nixon SJ, Zerial M, Parton RG (December 2005). "Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism". J. Biol. Chem. 280 (51): 42325–35. doi:10.1074/jbc.M506651200. PMID 16207721. 
  6. ^ Ozeki S, Cheng J, Tauchi-Sato K, Hatano N, Taniguchi H, Fujimoto T (June 2005). "Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane". J. Cell. Sci. 118 (Pt 12): 2601–11. doi:10.1242/jcs.02401. PMID 15914536. 
  7. ^ Burré J, Beckhaus T, Corvey C, Karas M, Zimmermann H, Volknandt W (September 2006). "Synaptic vesicle proteins under conditions of rest and activation: analysis by 2-D difference gel electrophoresis". Electrophoresis 27 (17): 3488–96. doi:10.1002/elps.200500864. PMID 16944461. 
  8. ^ Takamori S, Holt M, Stenius K, Lemke EA, Grønborg M, Riedel D, Urlaub H, Schenck S, Brügger B, Ringler P, Müller SA, Rammner B, Gräter F, Hub JS, De Groot BL, Mieskes G, Moriyama Y, Klingauf J, Grubmüller H, Heuser J, Wieland F, Jahn R (November 2006). "Molecular anatomy of a trafficking organelle". Cell 127 (4): 831–46. doi:10.1016/j.cell.2006.10.030. PMID 17110340. 
  9. ^ Vazquez-Martinez R, Cruz-Garcia D, Duran-Prado M, Peinado JR, Castaño JP, Malagon MM (July 2007). "Rab18 inhibits secretory activity in neuroendocrine cells by interacting with secretory granules". Traffic 8 (7): 867–82. doi:10.1111/j.1600-0854.2007.00570.x. PMID 17488286. 

[edit] Further reading

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