[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/rab8a-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/rab8a-wikipedia\/","headline":"RAB8A – Wikipedia","name":"RAB8A – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Ras-related protein Rab-8A is a protein","datePublished":"2022-04-24","dateModified":"2022-04-24","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/b\/b0\/PDB_2fu5_EBI.jpg\/180px-PDB_2fu5_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/b\/b0\/PDB_2fu5_EBI.jpg\/180px-PDB_2fu5_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/rab8a-wikipedia\/","about":["Wiki"],"wordCount":5674,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensRas-related protein Rab-8A is a protein that in humans is encoded by the RAB8A gene.[5][6][7]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Interactions[edit]References[edit]Further reading[edit]Function[edit]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 demonstrated. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.[7]Interactions[edit]RAB8A has been shown to interact with Optineurin[8] and MAP4K2.[9]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000167461 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003037 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Nimmo ER, Sanders PG, Padua RA, Hughes D, Williamson R, Johnson KJ (Aug 1991). “The MEL gene: a new member of the RAB\/YPT class of RAS-related genes”. Oncogene. 6 (8): 1347\u201351. PMID\u00a01886711.^ Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K (Oct 1993). “Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane”. The Journal of Cell Biology. 123 (1): 35\u201345. doi:10.1083\/jcb.123.1.35. PMC\u00a02119815. PMID\u00a08408203.^ a b “Entrez Gene: RAB8A RAB8A, member RAS oncogene family”.^ Hattula K, Per\u00e4nen J (2000). “FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis”. Current Biology. 10 (24): 1603\u20136. doi:10.1016\/S0960-9822(00)00864-2. PMID\u00a011137014. S2CID\u00a012836037.^ Ren M, Zeng J, De Lemos-Chiarandini C, Rosenfeld M, Adesnik M, Sabatini DD (May 1996). “In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase”. Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 5151\u20135. Bibcode:1996PNAS…93.5151R. doi:10.1073\/pnas.93.10.5151. PMC\u00a039423. PMID\u00a08643544.Further reading[edit]Newport J, Roemer MI (Mar 1975). “Comparative perinatal mortality under medical care foundations and other delivery models”. Inquiry. 12 (1): 10\u20137. PMID\u00a0123217.Nimmo E, Padua RA, Hughes D, Brook JD, Williamson R, Johnson KJ (Mar 1989). “Confirmation and refinement of the localisation of the c-MEL locus on chromosome 19 by physical and genetic mapping”. Human Genetics. 81 (4): 382\u20134. doi:10.1007\/BF00283697. PMID\u00a02564840. S2CID\u00a025002878.Zahraoui A, Joberty G, Arpin M, Fontaine JJ, Hellio R, Tavitian A, Louvard D (Jan 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”. The Journal of Cell Biology. 124 (1\u20132): 101\u201315. doi:10.1083\/jcb.124.1.101. PMC\u00a02119893. PMID\u00a08294494.Joberty G, Tavitian A, Zahraoui A (Sep 1993). “Isoprenylation of Rab proteins possessing a C-terminal CaaX motif”. FEBS Letters. 330 (3): 323\u20138. doi:10.1016\/0014-5793(93)80897-4. PMID\u00a08375503. S2CID\u00a029047580.Ren M, Zeng J, De Lemos-Chiarandini C, Rosenfeld M, Adesnik M, Sabatini DD (May 1996). “In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase”. Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 5151\u20135. Bibcode:1996PNAS…93.5151R. doi:10.1073\/pnas.93.10.5151. PMC\u00a039423. PMID\u00a08643544.B\u00e4hler M, Kehrer I, Gordon L, Stoffler HE, Olsen AS (Jul 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\u20139. doi:10.1006\/geno.1997.4776. PMID\u00a09226381.Wilson AL, Erdman RA, Castellano F, Maltese WA (Aug 1998). “Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases”. The Biochemical Journal. 333 (Pt 3): 497\u2013504. doi:10.1042\/bj3330497. PMC\u00a01219609. PMID\u00a09677305.Bao S, Zhu J, Garvey WT (Nov 1998). “Cloning of Rab GTPases expressed in human skeletal muscle: studies in insulin-resistant subjects”. Hormone and Metabolic Research. 30 (11): 656\u201362. doi:10.1055\/s-2007-978953. PMID\u00a09918381.Shisheva A, Chinni SR, DeMarco C (Sep 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\u201321. doi:10.1021\/bi990200r. PMID\u00a010512627.Hattula K, Per\u00e4nen J (2001). “FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis”. Current Biology. 10 (24): 1603\u20136. doi:10.1016\/S0960-9822(00)00864-2. PMID\u00a011137014. S2CID\u00a012836037.Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (Mar 2002). “The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain”. The Journal of Biological Chemistry. 277 (11): 9212\u20138. doi:10.1074\/jbc.M112414200. PMID\u00a011773082.Hattula K, Furuhjelm J, Arffman A, Per\u00e4nen J (Sep 2002). “A Rab8-specific GDP\/GTP exchange factor is involved in actin remodeling and polarized membrane transport”. Molecular Biology of the Cell. 13 (9): 3268\u201380. doi:10.1091\/mbc.E02-03-0143. PMC\u00a0124888. PMID\u00a012221131.Fukuda M (Apr 2003). “Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A\/Rab27A recognition by Rim2”. The Journal of Biological Chemistry. 278 (17): 15373\u201380. doi:10.1074\/jbc.M212341200. PMID\u00a012578829.Lau AS, Mruk DD (Apr 2003). “Rab8B GTPase and junction dynamics in the testis”. Endocrinology. 144 (4): 1549\u201363. doi:10.1210\/en.2002-220893. PMID\u00a012639940.Linder MD, Uronen RL, H\u00f6ltt\u00e4-Vuori M, van der Sluijs P, Per\u00e4nen J, Ikonen E (Jan 2007). “Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells”. Molecular Biology of the Cell. 18 (1): 47\u201356. doi:10.1091\/mbc.E06-07-0575. PMC\u00a01751315. PMID\u00a017050734.PDB gallery2fu5: structure of Rab8 in complex with MSS4       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/rab8a-wikipedia\/#breadcrumbitem","name":"RAB8A – Wikipedia"}}]}]