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RAB18

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(Redirected from RAB18 (gene))
RAB18
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRAB18, RAB18LI1, WARBM3, member RAS oncogene family
External IDsOMIM: 602207; MGI: 102790; HomoloGene: 40765; GeneCards: RAB18; OMA:RAB18 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001256410
NM_001256411
NM_001256412
NM_001256415
NM_021252

NM_001278447
NM_181070

RefSeq (protein)

NP_001243339
NP_001243340
NP_001243341
NP_001243344
NP_067075

NP_001265376
NP_851415

Location (UCSC)Chr 10: 27.5 – 27.54 MbChr 18: 6.73 – 6.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras-related protein Rab-18 is a protein that in humans is encoded by the RAB18 gene.[5][6] It is a member of the Rab family of Ras-related small GTPases.[7]

Rab18 is a ubiquitously expressed protein with particularly high expression in the brain.[8] Rab18 was first characterised as an endosomal protein in epithelial cells of mouse kidney and intestines.[8] 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.[7][9][10] In the brain, Rab18 has been isolated in association with synaptic vesicles[11][12] and has been observed to localise to secretory granules in neuroendocrine cells.[13]

Mutations in RAB18, RAB3GAP1, RAB3GAP2, or TBC1D20 are thought to cause Warburg Micro syndrome by disrupting RAB18 function. RAB3GAP1, RAB3GAP2, and TBC1D20 genes offer instructions for creating proteins that regulate RAB18.[14] The RAB3GAP1 and RAB3GAP2 proteins interact and create a guanine–nucleotide exchange factor complex that activates RAB18. The TBC1D20 protein may inactivate RAB18 by acting as a GTPase-activating protein for it.[14][15]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000099246Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000073639Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 31093183.
  6. ^ "Entrez Gene: RAB18 RAB18, member RAS oncogene family".
  7. ^ a b 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.
  8. ^ 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" (PDF). J. Cell Sci. 107 (12): 3437–48. doi:10.1242/jcs.107.12.3437. PMID 7706395.
  9. ^ 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" (PDF). J. Biol. Chem. 280 (51): 42325–35. doi:10.1074/jbc.M506651200. PMID 16207721. S2CID 30398568.
  10. ^ 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.
  11. ^ 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. S2CID 43618245.
  12. ^ 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. hdl:11858/00-001M-0000-0012-E357-D. PMID 17110340. S2CID 6703431.
  13. ^ 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. S2CID 9987968.
  14. ^ a b "RAB18 deficiency: MedlinePlus Genetics". Retrieved 27 September 2023.
  15. ^ Handley MT, Carpanini SM, Mali GR, Sidjanin DJ, Aligianis IA, Jackson IJ, FitzPatrick DR (2015). "Warburg Micro syndrome is caused by RAB18 deficiency or dysregulation". Open Biology. 5 (6). doi:10.1098/rsob.150047. PMC 4632505. PMID 26063829. 150047.

Further reading

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