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ANLN
Anillin is a conserved protein implicated in cytoskeletal dynamics during cellularization and cytokinesis. The ''ANLN'' gene in humans and the scraps gene in ''Drosophila'' encode Anillin.〔Piekny, A. J., & Maddox, A. S. (2010). The myriad roles of Anillin during cytokinesis. Semin Cell Dev Biol, 21(9), 881-891. doi: 10.1016/j.semcdb.2010.08.002〕 In 1989, anillin was first isolated in embryos of ''Drosophila melanogaster''. It was identified as an F-actin binding protein.〔Zhang, L., & Maddox, A. S. (2010). Anillin. Curr Biol, 20(4), 135-136. doi: 10.1016/j.cub.2009.12.017〕 Six years later, the anillin gene was cloned from cDNA originating from a Drosophila ovary. Staining with anti-anillin (Antigen 8) antibody showed the anillin localizes to the nucleus during interphase and to the contractile ring during cytokinesis.〔Field, C. M., & Alberts, B. M. (1995). Anillin, a Contractile Ring Protein That Cycles from the Nucleus to the Cell Cortex. The Journal of Cell Biology, 131(1), 165-178.〕 These observations agree with further research that found anillin in high concentrations near the cleavage furrow coinciding with RhoA, a key regulator of contractile ring formation.〔Piekny, A. J., & Glotzer, M. (2008). Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. Curr Biol, 18(1), 30-36. doi: 10.1016/j.cub.2007.11.068〕
The name of the protein anillin originates from a Spanish word, ''anillo''. ''Anillo'' means ring and shows that the name anillin references the observed enrichment of anillins at the contractile ring during cytokinesis. Anillins are also enriched at other actomyosin rings, most significantly, those at the leading edge of the Drosophila embryo during cellularization. These actomyosin rings invaginate to separate all nuclei for one another in the syncytial blastoderm.〔Piekny, A. J., & Maddox, A. S. (2010). The myriad roles of Anillin during cytokinesis. Semin Cell Dev Biol, 21(9), 881-891. doi: 10.1016/j.semcdb.2010.08.002〕
==Structure==
Anillin has a unique multi-domain structure. At the N-terminus, there is an actin- and myosin-binding domain. At the C-terminus, there is a PH domain. The PH domain is conserved and essential for anillin functionality.〔Piekny, A. J., & Glotzer, M. (2008). Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. Curr Biol, 18(1), 30-36. doi: 10.1016/j.cub.2007.11.068〕 The human anillin cDNA, located on Chr7, encodes a 1,125–amino acid protein with a predicted molecular mass of 124 kD and a pI of 8.1. The mouse anillin gene is located on Chr9.〔Oegema, K., Savovian, M. S., Mitchison, T. J., & Field, C. M. (2000). Functional Analysis of a Human Homologue of the Drosophila Actin Binding Protein Anillin Suggest a Role in Cytokinesis. The Journal of Cell Biology, 150(3), 539-551.〕
There are also numerous anillin-like protein homologues found outside of metazoans. In ''Schizosaccharomyces pombe'' (fission yeast), there are Mid1p and Mid2p. These two anillin-like proteins do not have any overlap in their functions. Mid1p has been characterized as a key regulator in cytokinesis, responsible for arranging contractile ring assembly and positioning.〔Saha, S., & Pollard, T. D. (2012). Characterization of structural and functional domains of the anillin-related protein Mid1p that contribute to cytokinesis in fission yeast. Mol Biol Cell, 23(20), 3993-4007. doi: 10.1091/mbc.E12-07-0536〕 Mid2p acts later in cytokinesis to organize septins during septation, or the invagination of inner membranes, outer membranes, and the cell wall that occurs in order to separate daughter cells completely.〔Tasto, J. J., Morrell, J. L., & Gould, K. L. (2003). An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation. J Cell Biol, 160(7), 1093-1103. doi: 10.1083/jcb.200211126〕 ''Saccharomyces cerevisiae'' (budding yeast) also have two anillin-like proteins, Boi1p and Boi2p. Boi1p and Boi2p localize to the nucleus and contractile ring at the bud neck, respectively. They are essential for cell growth and bud formation.〔Toya, M., Iino, Y., & Yamamoto, M. (1999). Fission Yeast Pob1p, Which Is Homologous to Budding Yeast Boi Proteins and Exhibits Subcellular Localization Close to Actin Patches, Is Essential for Cell Elongation and Separation. Mol Biol Cell, 10(8), 2745-2757.〕
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