Structural highlights
Function
ARL2_HUMAN Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle.[1] [2] [3] [4] [5]
References
- ↑ Bhamidipati A, Lewis SA, Cowan NJ. ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J Cell Biol. 2000 May 29;149(5):1087-96. PMID:10831612
- ↑ Zhou C, Cunningham L, Marcus AI, Li Y, Kahn RA. Arl2 and Arl3 regulate different microtubule-dependent processes. Mol Biol Cell. 2006 May;17(5):2476-87. Epub 2006 Mar 8. PMID:16525022 doi:http://dx.doi.org/E05-10-0929
- ↑ Veltel S, Kravchenko A, Ismail S, Wittinghofer A. Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex. FEBS Lett. 2008 Jul 23;582(17):2501-7. Epub 2008 Jun 25. PMID:18588884 doi:http://dx.doi.org/S0014-5793(08)00550-4
- ↑ Muromoto R, Sekine Y, Imoto S, Ikeda O, Okayama T, Sato N, Matsuda T. BART is essential for nuclear retention of STAT3. Int Immunol. 2008 Mar;20(3):395-403. doi: 10.1093/intimm/dxm154. Epub 2008 Jan, 29. PMID:18234692 doi:http://dx.doi.org/10.1093/intimm/dxm154
- ↑ Tian G, Thomas S, Cowan NJ. Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity. Cytoskeleton (Hoboken). 2010 Nov;67(11):706-14. doi: 10.1002/cm.20480. PMID:20740604 doi:http://dx.doi.org/10.1002/cm.20480