Mitotic activity of survivin is regulated by acetylation at K129

References

• Ambrosini G, Adida C, Sirugo G, Altieri DC. Induction of apoptosis and inhibition of cell proliferation by survivin gene targeting. J Biol Chem 1998; 273:11177-82; PMID:9556606; http://dx.doi.org/10.1074/jbc.273.18.11177
   PubMed Web of Science ®Google Scholar
• Carvalho A, Carmena M, Sambade C, Earnshaw WC, Wheatley SP. Survivin is required for stable checkpoint activation in response to loss of spindle tension in HeLa cells. J Cell Sci 2003; 116:2987-98; PMID:12783991; http://dx.doi.org/10.1242/jcs.00612
   PubMed Web of Science ®Google Scholar
• Lens SM, Wolthuis RM, Klompmaker R, Kauw J, Agami R, Brummelkamp T, Kops G, Medema RH. Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension. EMBO J 2003; 22:2934-47; PMID:12805209; http://dx.doi.org/10.1093/emboj/cdg307
   PubMed Web of Science ®Google Scholar
• Uren AG, Wong L, Pakusch M, Fowler KJ, Burrows FJ, Vaux DL, Choo KHA. Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype. Curr Biol 2000; 10:1319-28; PMID:11084331; http://dx.doi.org/10.1016/S0960-9822(00)00769-7
   PubMed Web of Science ®Google Scholar
• Fortugno P, Wall NR, Giodini A, O'Connor DS, Plescia J, Padgett KM, Tognin S, Marchisio PC, Altieri DC. Survivin exists in immunochemically distinct subcellular pools and is involved in spindle microtubule function. J Cell Sci 2002; 115:575-85; PMID:11861764
   PubMed Web of Science ®Google Scholar
• Wang HJ, Holloway MP, Ma L, Cooper ZA, Riolo M, Samkari A, Elenitoba-Johnson KSJ, Chin YE, Altura RA. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem 2010; 285:36129-37; PMID:20826784; http://dx.doi.org/10.1074/jbc.M110.152777
   PubMed Web of Science ®Google Scholar
• Wang F, Dai J, Daum JR, Niedzialkowska E, Banerjee B, Stukenberg PT, Gorbsky GJ, Higgins JMG. Histone H3 Thr-3 phosphorylation by haspin positions aurora B at centromeres in mitosis. Science 2010; 330:231-5; PMID:20705812; http://dx.doi.org/10.1126/science.1189435
   PubMed Web of Science ®Google Scholar
• Wheatley SP, Barrett RMA, Andrews PD, Medema RH, Morley SJ, Swedlow JR, Lens SMA. Phosphorylation of aurora-B negatively regulates survivin function during mitosis. Cell Cycle 2007; 6:1220-30; PMID:17457057; http://dx.doi.org/10.4161/cc.6.10.4179
   PubMed Web of Science ®Google Scholar
• Wall NR, O'Connor DS, Plescia J, Pommier Y, Altieri DC. Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumour cell apoptosis. Cancer Res 2003; 63:230-5; PMID:12517802
   PubMed Web of Science ®Google Scholar
• Barrett RMA, Osborne TP, Wheatley SP. Phosphorylation of survivin at threonine 34 inhibits its mitotic function and enhances its cytoprotective activity. Cell Cycle 2009; 8:278-83; PMID:19158485; http://dx.doi.org/10.4161/cc.8.2.7587
   PubMed Web of Science ®Google Scholar
• Colnaghi R, Wheatley SP. Liaisons between survivin and plk1 during cell division and cell death. J Biol Chem 2010; 285:22592-604; PMID:20427271; http://dx.doi.org/10.1074/jbc.M109.065003
   PubMed Web of Science ®Google Scholar
• Vong QP, Cao K, Li HY, Iglesias P, Zheng Y. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science 2005; 310:1499-504; PMID:16322459; http://dx.doi.org/10.1126/science.1120160
   PubMed Web of Science ®Google Scholar
• Honda R, Korner R, Nigg EA. Exploring the functional interactions between aurora B, INCENP, and survivin in mitosis. Mol Biol Cell 2003; 14:3325-41; PMID:12925766; http://dx.doi.org/10.1091/mbc.E02-11-0769
   PubMed Web of Science ®Google Scholar
• Jeyaprakash AA, Klein UR, Lindner D, Ebert J, Nigg EA, Conti E. Structure of a survivin-borealin-INCENP core complex reveals how chromosomal passengers travel together. Cell 2007; 131:271-85; PMID:17956729; http://dx.doi.org/10.1016/j.cell.2007.07.045
   PubMed Web of Science ®Google Scholar
• Aljaberi A, Webster J, Wheatley S. Analysis of the functional repertoire of a mutant form of survivin, K129E, which has been linked to lung cancer. Cancer Cell Int 2014; 14:78; MS ID: 1190384217133615; PMID:25788861; http://dx.doi.org/10.1186/s12935-014-0078-8
   PubMed Web of Science ®Google Scholar
• Jang JS, HKim KM, Kang KH, Choi JE, Lee WK, Kim CH, Kang YM, Kam S, Kim I-S, Jun JE, et al. Polymorphisms in the survivin gene and the risk of lung cancer. Lung Cancer 2008; 60:31-9; PMID:17961802; http://dx.doi.org/10.1016/j.lungcan.2007.09.008
   PubMed Web of Science ®Google Scholar
• Verdecia MA, Huang H, Dutil E, Kaiser DA, Hunter T, Noel JP. Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. Nat Struct Biol 2000; 7:602-8; PMID:10876248; http://dx.doi.org/10.1038/77929
   PubMedGoogle Scholar
• Colnaghi R, Connell CM, Barrett RMA, Wheatley SP. Separating the anti-apoptotic and mitotic roles of survivin. J Biol Chem 2006; 281:33450-6; PMID:16950794; http://dx.doi.org/10.1074/jbc.C600164200
   PubMed Web of Science ®Google Scholar
• Connell CM, Colnaghi R, Wheatley SP. Nuclear survivin has reduced stability and is not. J Biol Chem 2008; 238:3289-96; PMID:18057009; http://dx.doi.org/10.1074/jbc.M704461200
   PubMed Web of Science ®Google Scholar
• Glozak MA, Sengupta N, Zhang X, Seto E. Acetylation and deacetylation of non-histone proteins. Gene 2005; 363:15-23; PMID:16289629; http://dx.doi.org/10.1016/j.gene.2005.09.010
   PubMed Web of Science ®Google Scholar
• Kozako T, Suzuki T, Yoshimitsu M, Arima N, Honda S-I, Soeda S. Anticancer agents targeted to sirtuins. Molecules 2014; 19: 20295-313; PMID:25486244; http://dx.doi.org/10.3390/molecules191220295
   PubMed Web of Science ®Google Scholar
• Ishii S, Kurasawa Y, Wong J, Yu-Lee L-Y. Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment. PNAS 2008; 105:4179-84; PMID:18326024; http://dx.doi.org/10.1073/pnas.0710140105
   PubMed Web of Science ®Google Scholar
• Park I, Lee H-O, Choi E, Lee Y-K, Kwon M-S, Min J, Park P-G, Lee S, Kong Y-Y, Gong G, et al. Loss of BubR1 acetylation causes defects in spindle assembly checkpoint signaling and promotes tumor formation. J Cell Biol 2013; 202:295-309; PMID:23878276; http://dx.doi.org/10.1083/jcb.201210099
   PubMed Web of Science ®Google Scholar
• Chuang C, Lin S-H, Huang F, Pan J, Josic D, Yu-Lee L-Y. Acetylation of RNA processing proteins and cell cycle proteins in mitosis. J Proteome Res 2010; 9:4554-64; PMID:20812760; http://dx.doi.org/10.1021/pr100281h
   PubMed Web of Science ®Google Scholar
• Li Y, Kao GD, Garcia BA, Shabanowitz J, Hunt DF, Qin J, Phelan C, Lazar MA. A novel histone deacetylase pathway regulates mitosis by modulating aurora B kinase activity. Genes Dev 2006; 20:2566-79; PMID:16980585; http://dx.doi.org/10.1101/gad.1455006
   PubMed Web of Science ®Google Scholar
• Riolo MT, Cooper ZA, Holloway MP, Cheng Y, Bianchi C, Yakirevich E, Ma L, Chin YE, Altura RA. Histone deacetylase 6 (HDAC6) deacetylates survivin for its nuclear export in breast cancer. J Biol Chem 2012; 287:10885-93; PMID:22334690; http://dx.doi.org/10.1074/jbc.M111.308791
   PubMed Web of Science ®Google Scholar
• Yakirevich E, Samkari A, Holloway MP, Lu S, Singh K, Yu J, Fenton MA, Altura RA. Total survivin and acetylated survivin correlate with distinct molecular subtypes of breast cancer. Hum Pathol 2012; 43:865-73; PMID:22055399; http://dx.doi.org/10.1016/j.humpath.2011.07.014
   PubMed Web of Science ®Google Scholar
• Lens SM, Medema RH. The survivin/Aurora B complex: its role in coordinating tension and attachment. Cell Cycle 2003; 2:507-10; PMID:14504461; http://dx.doi.org/10.4161/cc.2.6.559
   PubMed Web of Science ®Google Scholar
• Knauer SK, Bier C, Habtemichael N, Stauber RH. The survivin-Crm1 interaction is essential for chromosomal passenger complex localization and function. EMBO Rep 2006; 12:1259-65; PMID:17099693; http://dx.doi.org/10.1038/sj.embor.7400824
   PubMed Web of Science ®Google Scholar
• Engelsma D, Rodriguez JA, Fish A, Giaccone G, Fornerod M. Homodimerization antagonizes nuclear export of survivin. Traffic 2007; 11:1495-502; PMID:17714426; http://dx.doi.org/10.1111/j.1600-0854.2007.00629.x
   PubMed Web of Science ®Google Scholar
• Arora V, Cheung HH, Plenchette S, Micali OC, Liston P, Korneluk RG. Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 complex. J Biol Chem 2007; 282:26202-9; PMID:17613533; http://dx.doi.org/10.1074/jbc.M700776200
   PubMed Web of Science ®Google Scholar
• Wheatley SP, Henzing AJ, Dodson H, Khaled W, Earnshaw WC. Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to INCENP in vivo. J Biol Chem 2004; 279:5655-60; PMID:14610074; http://dx.doi.org/10.1074/jbc.M311299200
   PubMed Web of Science ®Google Scholar