Biology:ARL2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
ADP-ribosylation factor-like protein 2 is a protein that in humans is encoded by the ARL2 gene.[1][2][3]
Function
- The ADP-ribosylation factor (ARF) genes are small GTP-binding proteins of the RAS superfamily. ARL2 is a member of a functionally distinct group of ARF-like genes.[3]
- In photoreceptors, ARL2 participates in the trafficking of lipidated membrane-associated proteins.[4]
- There is an evidence that increased activity of ARL2 protein is strongly correlated with increased mitochondria fusion, while loss of ARL2 activity results in a decreased rate of fusion.[5]
Interactions
ARL2 has been shown to interact with Protein unc-119 homolog,[6] TBCD[7][8] and PDE6D.[9][10]
References
- ↑ "Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8952–6. November 1993. doi:10.1073/pnas.90.19.8952. PMID 8415637. Bibcode: 1993PNAS...90.8952C.
- ↑ "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Res. 7 (7): 725–35. September 1997. doi:10.1101/gr.7.7.725. PMID 9253601.
- ↑ 3.0 3.1 "Entrez Gene: ARL2 ADP-ribosylation factor-like 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=402.
- ↑ Hanke-Gogokhia, C.; Zhang, H.; Frederick, J. M.; Baehr, W. (2016). "The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors". Advances in Experimental Medicine and Biology 854: 655–661. doi:10.1007/978-3-319-17121-0_87. ISBN 978-3-319-17120-3. PMID 26427472. https://pubmed.ncbi.nlm.nih.gov/26427472/.
- ↑ Newman, L. E.; Schiavon, C. R.; Turn, R. E.; Kahn, R. A. (2017). "The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space". Cellular Logistics 7 (3): e1340104. doi:10.1080/21592799.2017.1340104. PMID 28944094.
- ↑ "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. January 2003. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357.
- ↑ "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. October 2003. doi:10.1074/jbc.M308678200. PMID 12912990.
- ↑ "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. May 2000. doi:10.1083/jcb.149.5.1087. PMID 10831612.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. May 2002. doi:10.1093/emboj/21.9.2095. PMID 11980706.
External links
- Human ARL2 genome location and ARL2 gene details page in the UCSC Genome Browser.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. 2000. doi:10.1083/jcb.149.5.1087. PMID 10831612.
- "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter". Mol. Biol. Cell 13 (1): 71–83. 2002. doi:10.1091/mbc.01-05-0245. PMID 11809823.
- "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. 2002. doi:10.1093/emboj/21.9.2095. PMID 11980706.
- "The C. elegans evl-20 gene is a homolog of the small GTPase ARL2 and regulates cytoskeleton dynamics during cytokinesis and morphogenesis". Dev. Cell 2 (5): 579–91. 2002. doi:10.1016/S1534-5807(02)00146-6. PMID 12015966.
- "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. 2003. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357.
- "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. 2003. doi:10.1074/jbc.M308678200. PMID 12912990.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Arl2 and Arl3 regulate different microtubule-dependent processes". Mol. Biol. Cell 17 (5): 2476–87. 2006. doi:10.1091/mbc.E05-10-0929. PMID 16525022.
- "ADP ribosylation factor like 2 (Arl2) protein influences microtubule dynamics in breast cancer cells". Exp. Cell Res. 313 (3): 473–85. 2007. doi:10.1016/j.yexcr.2006.10.024. PMID 17188265.
PDB gallery | |
|---|---|
|
 |
