RAB8A

From Wikipedia, the free encyclopedia

RAB8A, member RAS oncogene family

PDB rendering based on 2fu5.

Available structures: 2fu5

Identifiers

Symbol(s)

RAB8A; MEL; RAB8

External IDs

OMIM: 165040 MGI: 96960 HomoloGene: 21111

Gene ontology
Molecular Function:	• nucleotide binding • GTP binding
Cellular Component:	• membrane
Biological Process:	• small GTPase mediated signal transduction • protein transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005370 (mRNA)
NP_005361 (protein)

XM_981797 (mRNA)
XP_986891 (protein)

Location

Chr 19: 16.08 - 16.11 Mb

Chr 8: 75.09 - 75.11 Mb

Pubmed search

[1]

[2]

RAB8A, member RAS oncogene family, also known as RAB8A, is a human gene.^[1]

The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all the RAS proteins. The putative effector-binding site of this protein is similar to that of the RAB/YPT proteins. However, this protein contains a C-terminal CAAX motif that is characteristic of many RAS superfamily members but which is not found in YPT1 and the majority of RAB proteins. Although this gene was isolated as a transforming gene from a melanoma cell line, no linkage between MEL and malignant melanoma has been demonstrable. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.^[1]

[edit] References

^ ^a ^b Entrez Gene: RAB8A RAB8A, member RAS oncogene family.

[edit] Further reading

Newport J, Roemer MI (1975). "Comparative perinatal mortality under medical care foundations and other delivery models.". Inquiry : a journal of medical care organization, provision and financing 12 (1): 10–7. PMID 123217.
Nimmo ER, Sanders PG, Padua RA, et al. (1991). "The MEL gene: a new member of the RAB/YPT class of RAS-related genes.". Oncogene 6 (8): 1347–51. PMID 1886711.
Nimmo E, Padua RA, Hughes D, et al. (1989). "Confirmation and refinement of the localisation of the c-MEL locus on chromosome 19 by physical and genetic mapping.". Hum. Genet. 81 (4): 382–4. PMID 2564840.
Zahraoui A, Joberty G, Arpin M, et al. (1994). "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells.". J. Cell Biol. 124 (1-2): 101–15. PMID 8294494.
Joberty G, Tavitian A, Zahraoui A (1993). "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif.". FEBS Lett. 330 (3): 323–8. PMID 8375503.
Huber LA, Pimplikar S, Parton RG, et al. (1993). "Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane.". J. Cell Biol. 123 (1): 35–45. PMID 8408203.
Ren M, Zeng J, De Lemos-Chiarandini C, et al. (1996). "In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase.". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 5151–5. PMID 8643544.
Bähler M, Kehrer I, Gordon L, et al. (1997). "Physical mapping of human myosin-IXB (MYO9B), the human orthologue of the rat myosin myr 5, to chromosome 19p13.1.". Genomics 43 (1): 107–9. doi:10.1006/geno.1997.4776. PMID 9226381.
Wilson AL, Erdman RA, Castellano F, Maltese WA (1998). "Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases.". Biochem. J. 333 ( Pt 3): 497–504. PMID 9677305.
Bao S, Zhu J, Garvey WT (1999). "Cloning of Rab GTPases expressed in human skeletal muscle: studies in insulin-resistant subjects.". Horm. Metab. Res. 30 (11): 656–62. PMID 9918381.
Shisheva A, Chinni SR, DeMarco C (1999). "General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications.". Biochemistry 38 (36): 11711–21. PMID 10512627.
Hattula K, Peränen J (2001). "FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis.". Curr. Biol. 10 (24): 1603–6. PMID 11137014.
Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain.". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
Hattula K, Furuhjelm J, Arffman A, Peränen J (2003). "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport.". Mol. Biol. Cell 13 (9): 3268–80. doi:10.1091/mbc.E02-03-0143. PMID 12221131.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Fukuda M (2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2.". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
Lau AS, Mruk DD (2003). "Rab8B GTPase and junction dynamics in the testis.". Endocrinology 144 (4): 1549–63. PMID 12639940.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Linder MD, Uronen RL, Hölttä-Vuori M, et al. (2007). "Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells.". Mol. Biol. Cell 18 (1): 47–56. doi:10.1091/mbc.E06-07-0575. PMID 17050734.