アニリン (タンパク質)
(an ln から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2023/12/12 04:10 UTC 版)
アニリン（英: anillin）は、細胞化（cellularization）や細胞質分裂の際の細胞骨格のダイナミクスに関係するタンパク質であり、ヒトではANLN遺伝子、ショウジョウバエではscraps遺伝子にコードされる[5]。アニリンは1989年にキイロショウジョウバエDrosophila melanogasterの胚から初めて単離され、F-アクチン結合タンパク質として同定された[6]。6年後、アニリンの遺伝子はショウジョウバエ卵巣由来のcDNAからクローニングされた。抗アニリン（Antigen 8）抗体を用いた染色によって、アニリンは間期には核に、細胞質分裂時には収縮環に局在していることが示された[7]。その後の研究によって、アニリンは分裂溝の近傍で、収縮環形成の重要な調節因子であるRhoAとともに高濃度で存在することが明らかにされている[8]。
- ^ a b c GRCh38: Ensembl release 89: ENSG00000011426 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036777 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ a b c d Piekny AJ, Maddox AS (December 2010). “The myriad roles of Anillin during cytokinesis”. Seminars in Cell & Developmental Biology 21 (9): 881–91. doi:10.1016/j.semcdb.2010.08.002. PMID 20732437.
- ^ a b Zhang L, Maddox AS (February 2010). “Anillin”. Current Biology 20 (4): R135-6. doi:10.1016/j.cub.2009.12.017. PMID 20178751.
- ^ a b Field CM, Alberts BM (October 1995). “Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex”. The Journal of Cell Biology 131 (1): 165–78. doi:10.1083/jcb.131.1.165. PMC 2120607. PMID 7559773.
- ^ a b Piekny AJ, Glotzer M (January 2008). “Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis”. Current Biology 18 (1): 30–6. doi:10.1016/j.cub.2007.11.068. PMID 18158243.
- ^ a b Oegema K, Savoian MS, Mitchison TJ, Field CM (August 2000). “Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis”. The Journal of Cell Biology 150 (3): 539–52. doi:10.1083/jcb.150.3.539. PMC 2175195. PMID 10931866.
- ^ Saha S, Pollard TD (October 2012). “Characterization of structural and functional domains of the anillin-related protein Mid1p that contribute to cytokinesis in fission yeast”. Molecular Biology of the Cell 23 (20): 3993–4007. doi:10.1091/mbc.E12-07-0536. PMC 3469515. PMID 22918954.
- ^ Tasto JJ, Morrell JL, Gould KL (March 2003). “An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation”. The Journal of Cell Biology 160 (7): 1093–103. doi:10.1083/jcb.200211126. PMC 2172762. PMID 12668659.
- ^ Toya M, Iino Y, Yamamoto M (August 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”. Molecular Biology of the Cell 10 (8): 2745–57. doi:10.1091/mbc.10.8.2745. PMC 25510. PMID 10436025.
- ^ a b Maddox AS, Habermann B, Desai A, Oegema K (June 2005). “Distinct roles for two C. elegans anillins in the gonad and early embryo”. Development 132 (12): 2837–48. doi:10.1242/dev.01828. PMID 15930113.
- ^ D'Avino PP, Takeda T, Capalbo L, Zhang W, Lilley KS, Laue ED, Glover DM (April 2008). “Interaction between Anillin and RacGAP50C connects the actomyosin contractile ring with spindle microtubules at the cell division site”. Journal of Cell Science 121 (Pt 8): 1151–8. doi:10.1242/jcs.026716. PMID 18349071.
- ^ a b Kučera O, Siahaan V, Janda D, Dijkstra SH, Pilátová E, Zatecka E, Diez S, Braun M, Lansky Z (2021). “Anillin propels myosin-independent constriction of actin rings”. Nature Communications 12 (1): 4595. Bibcode: 2021NatCo..12.4595K. doi:10.1038/s41467-021-24474-1. PMC 8319318. PMID 34321459.
- ^ Watanabe S, Okawa K, Miki T, Sakamoto S, Morinaga T, Segawa K, Arakawa T, Kinoshita M, Ishizaki T, Narumiya S (September 2010). “Rho and anillin-dependent control of mDia2 localization and function in cytokinesis”. Molecular Biology of the Cell 21 (18): 3193–204. doi:10.1091/mbc.E10-04-0324. PMC 2938385. PMID 20660154.
- ^ Straight AF, Field CM, Mitchison TJ (January 2005). “Anillin binds nonmuscle myosin II and regulates the contractile ring”. Molecular Biology of the Cell 16 (1): 193–201. doi:10.1091/mbc.E04-08-0758. PMC 539163. PMID 15496454.
- ^ Field CM, Coughlin M, Doberstein S, Marty T, Sullivan W (June 2005). “Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity”. Development 132 (12): 2849–60. doi:10.1242/dev.01843. PMID 15930114.
- ^ a b Goldbach P, Wong R, Beise N, Sarpal R, Trimble WS, Brill JA (May 2010). “Stabilization of the actomyosin ring enables spermatocyte cytokinesis in Drosophila”. Molecular Biology of the Cell 21 (9): 1482–93. doi:10.1091/mbc.E09-08-0714. PMC 2861608. PMID 20237160.
- ^ Versele M, Thorner J (August 2005). “Some assembly required: yeast septins provide the instruction manual”. Trends in Cell Biology 15 (8): 414–24. doi:10.1016/j.tcb.2005.06.007. PMC 1761124. PMID 16009555.
- ^ Kinoshita M, Field CM, Coughlin ML, Straight AF, Mitchison TJ (December 2002). “Self- and actin-templated assembly of Mammalian septins”. Developmental Cell 3 (6): 791–802. doi:10.1016/S1534-5807(02)00366-0. PMID 12479805.
- ^ Solski PA, Wilder RS, Rossman KL, Sondek J, Cox AD, Campbell SL, Der CJ (June 2004). “Requirement for C-terminal sequences in regulation of Ect2 guanine nucleotide exchange specificity and transformation”. The Journal of Biological Chemistry 279 (24): 25226–33. doi:10.1074/jbc.M313792200. PMID 15073184.
- ^ Glotzer M (January 2009). “The 3Ms of central spindle assembly: microtubules, motors and MAPs”. Nature Reviews. Molecular Cell Biology 10 (1): 9–20. doi:10.1038/nrm2609. PMC 2789570. PMID 19197328.
- ^ Gregory SL, Ebrahimi S, Milverton J, Jones WM, Bejsovec A, Saint R (January 2008). “Cell division requires a direct link between microtubule-bound RacGAP and Anillin in the contractile ring”. Current Biology 18 (1): 25–9. doi:10.1016/j.cub.2007.11.050. PMID 18158242.
- ^ Zhao WM, Fang G (September 2005). “Anillin is a substrate of anaphase-promoting complex/cyclosome (APC/C) that controls spatial contractility of myosin during late cytokinesis”. The Journal of Biological Chemistry 280 (39): 33516–24. doi:10.1074/jbc.M504657200. PMID 16040610.
- ^ Sisson JC, Field C, Ventura R, Royou A, Sullivan W (November 2000). “Lava lamp, a novel peripheral golgi protein, is required for Drosophila melanogaster cellularization”. The Journal of Cell Biology 151 (4): 905–18. doi:10.1083/jcb.151.4.905. PMC 2169433. PMID 11076973.
- ^ Hickson GR, O'Farrell PH (January 2008). “Rho-dependent control of anillin behavior during cytokinesis”. The Journal of Cell Biology 180 (2): 285–94. doi:10.1083/jcb.200709005. PMC 2213597. PMID 18209105.
- ^ Chuang HY, Ou YH (2014). Overexpression of anillin in colorectal cancer promoter the cell proliferation, cell mobility and cell invasion. Proceedings of the 105th Annual Meeting of the American Association for Cancer Research. San Diego, CA.
- ^ Wang G, Shen W, Cui L, Chen W, Hu X, Fu J (2016). “Overexpression of Anillin (ANLN) is correlated with colorectal cancer progression and poor prognosis”. Cancer Biomarkers 16 (3): 459–65. doi:10.3233/CBM-160585. PMID 27062703.
[続きの解説]
「アニリン (タンパク質)」の続きの解説一覧
- 1 アニリン (タンパク質)とは
- 2 アニリン (タンパク質)の概要
- 3 構造と機能
- 4 結合パートナー
- 5 疾患における役割
- アニリン (タンパク質)のページへのリンク
