Oxidation of Akt2 kinase promotes cell migration and regulates G₁-S transition in the cell cycle

References

• Woodgett JR. Recent advances in the protein kinase B signaling pathway. Curr Opin Cell Biol 2005; 17:150 - 157; PMID: 15780591; http://dx.doi.org/10.1016/j.ceb.2005.02.010
   PubMed Web of Science ®Google Scholar
• Brazil DP, Yang ZZ, Hemmings BA. Advances in protein kinase B signalling: AKTion on multiple fronts. Trends Biochem Sci 2004; 29:233 - 242; PMID: 15130559; http://dx.doi.org/10.1016/j.tibs.2004.03.006
   PubMed Web of Science ®Google Scholar
• Bellacosa A, Testa JR, Moore R, Larue L. A portrait of AKT kinases: human cancer and animal models depict a family with strong individualities. Cancer Biol Ther 2004; 3:268 - 275; PMID: 15034304; http://dx.doi.org/10.4161/cbt.3.3.703
   PubMed Web of Science ®Google Scholar
• Dummler B, Tschopp O, Hynx D, Yang ZZ, Dirnhofer S, Hemmings BA. Life with a single isoform of Akt: mice lacking Akt2 and Akt3 are viable but display impaired glucose homeostasis and growth deficiencies. Mol Cell Biol 2006; 26:8042 - 8051; PMID: 16923958; http://dx.doi.org/10.1128/MCB.00722-06
   PubMed Web of Science ®Google Scholar
• Peng XD, Xu PZ, Chen ML, Hahn-Windgassen A, Skeen J, Jacobs J, et al. Dwarfism, impaired skin development, skeletal muscle atrophy, delayed bone development and impeded adipogenesis in mice lacking Akt1 and Akt2. Genes Dev 2003; 17:1352 - 1365; PMID: 12782654; http://dx.doi.org/10.1101/gad.1089403
   PubMed Web of Science ®Google Scholar
• Franke TF. Intracellular signaling by Akt: bound to be specific. Sci Signal 2008; 1:29; PMID: 18560018; http://dx.doi.org/10.1126/scisignal.124pe29
   PubMed Web of Science ®Google Scholar
• Gonzalez E, McGraw TE. Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling. Proc Natl Acad Sci USA 2009; 106:7004 - 7009; PMID: 19372382; http://dx.doi.org/10.1073/pnas.0901933106
   PubMed Web of Science ®Google Scholar
• Santi SA, Lee H. The Akt isoforms are present at distinct subcellular locations. Am J Physiol Cell Physiol 2010; 298:580 - 591; PMID: 20018949; http://dx.doi.org/10.1152/ajpcell.00375.2009
   PubMed Web of Science ®Google Scholar
• Wani R, Qian J, Yin L, Bechtold E, King SB, Poole LB, et al. Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species. Proc Natl Acad Sci USA 2011; 108:10550 - 10555; PMID: 21670275; http://dx.doi.org/10.1073/pnas.1011665108
   PubMed Web of Science ®Google Scholar
• Ridley AJ, Schwartz MA, Burridge K, Firtel RA, Ginsberg MH, Borisy G, et al. Cell migration: integrating signals from front to back. Science 2003; 302:1704 - 1709; PMID: 14657486; http://dx.doi.org/10.1126/science.1092053
   PubMed Web of Science ®Google Scholar
• Merlot S, Firtel RA. Leading the way: Directional sensing through phosphatidylinositol-3-kinase and other signaling pathways. J Cell Sci 2003; 116:3471 - 3478; PMID: 12893811; http://dx.doi.org/10.1242/jcs.00703
   PubMed Web of Science ®Google Scholar
• Devreotes P, Janetopoulos C. Eukaryotic chemotaxis: distinctions between directional sensing and polarization. J Biol Chem 2003; 278:20445 - 20448; PMID: 12672811; http://dx.doi.org/10.1074/jbc.R300010200
   PubMed Web of Science ®Google Scholar
• Yoeli-Lerner M, Yiu GK, Rabinovitz I, Erhardt P, Jauliac S, Toker A. Akt blocks breast cancer cell motility and invasion through the transcription factor NFAT. Mol Cell 2005; 20:539 - 550; PMID: 16307918; http://dx.doi.org/10.1016/j.molcel.2005.10.033
   PubMed Web of Science ®Google Scholar
• Smits M, Nilsson J, Mir SE, van der Stoop PM, Hulleman E, Niers JM, et al. miR-101 is downregulated in glioblastoma resulting in EZH2-induced proliferation, migration and angiogenesis. Oncotarget 2010; 1:710 - 720; PMID: 21321380
   PubMed Web of Science ®Google Scholar
• Cha TL, Zhou BP, Xia W, Wu Y, Yang CC, Chen CT, et al. Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science 2005; 310:306 - 310; PMID: 16224021; http://dx.doi.org/10.1126/science.1118947
   PubMed Web of Science ®Google Scholar
• Arboleda MJ, Lyons JF, Kabbinavar FF, Bray MR, Snow BE, Ayala R, et al. Overexpression of AKT2/protein kinase Bbeta leads to upregulation of beta1 integrins, increased invasion and metastasis of human breast and ovarian cancer cells. Cancer Res 2003; 63:196 - 206; PMID: 12517798
   PubMed Web of Science ®Google Scholar
• Wang J, Wan W, Sun R, Liu Y, Sun X, Ma D, et al. Reduction of Akt2 expression inhibits chemotaxis signal transduction in human breast cancer cells. Cell Signal 2008; 20:1025 - 1034; PMID: 18353613; http://dx.doi.org/10.1016/j.cellsig.2007.12.023
   PubMed Web of Science ®Google Scholar
• Zhang B, Gu F, She C, Guo H, Li W, Niu R, et al. Reduction of Akt2 inhibits migration and invasion of glioma cells. Int J Cancer 2009; 125:585 - 595; PMID: 19330838; http://dx.doi.org/10.1002/ijc.24314
   PubMed Web of Science ®Google Scholar
• Chin YR, Toker A. Akt2 regulates expression of the actin-bundling protein palladin. FEBS Lett 2010; 584:4769 - 4774; PMID: 21050850; http://dx.doi.org/10.1016/j.febslet.2010.10.056
   PubMed Web of Science ®Google Scholar
• Cheng GZ, Zhang W, Wang LH. Regulation of cancer cell survival, migration and invasion by Twist: AKT2 comes to interplay. Cancer Res 2008; 68:957 - 960; PMID: 18281467; http://dx.doi.org/10.1158/0008-5472.CAN-07-5067
   PubMed Web of Science ®Google Scholar
• Chin YR, Toker A. The actin-bundling protein palladin is an Akt1-specific substrate that regulates breast cancer cell migration. Mol Cell 2010; 38:333 - 344; PMID: 20471940; http://dx.doi.org/10.1016/j.molcel.2010.02.031
   PubMed Web of Science ®Google Scholar
• Du K, Tsichlis PN. Regulation of the Akt kinase by interacting proteins. Oncogene 2005; 24:7401 - 7409; PMID: 16288287; http://dx.doi.org/10.1038/sj.onc.1209099
   PubMed Web of Science ®Google Scholar
• Yoeli-Lerner M, Toker A. Akt/PKB signaling in cancer: a function in cell motility and invasion. Cell Cycle 2006; 5:603 - 605; PMID: 16582622; http://dx.doi.org/10.4161/cc.5.6.2561
   PubMed Web of Science ®Google Scholar
• Zhou GL, Tucker DF, Bae SS, Bhatheja K, Birnbaum MJ, Field J. Opposing roles for Akt1 and Akt2 in Rac/Pak signaling and cell migration. J Biol Chem 2006; 281:36443 - 36453; PMID: 17012749; http://dx.doi.org/10.1074/jbc.M600788200
   PubMed Web of Science ®Google Scholar
• Higuchi M, Masuyama N, Fukui Y, Suzuki A, Gotoh Y. Akt mediates Rac/Cdc42-regulated cell motility in growth factor-stimulated cells and in invasive PTEN knockout cells. Curr Biol 2001; 11:1958 - 1962; PMID: 11747822; http://dx.doi.org/10.1016/S0960-9822(01)00599-1
   PubMed Web of Science ®Google Scholar
• Servant G, Weiner OD, Herzmark P, Balla T, Sedat JW, Bourne HR. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 2000; 287:1037 - 1040; PMID: 10669415; http://dx.doi.org/10.1126/science.287.5455.1037
   PubMed Web of Science ®Google Scholar
• Ho YP, Kuo CW, Hsu YT, Huang YS, Yew LP, Huang WF, et al. β-Actin is a downstream effector of the PI3K/AKT signaling pathway in myeloma cells. Mol Cell Biochem 2011; 348:129 - 139; PMID: 21069433; http://dx.doi.org/10.1007/s11010-010-0647-7
   PubMed Web of Science ®Google Scholar
• Vandermoere F, El Yazidi-Belkoura I, Demont Y, Slomianny C, Antol J, Lemoine J, et al. Proteomics exploration reveals that actin is a signaling target of the kinase Akt. Mol Cell Proteomics 2007; 6:114 - 124; PMID: 17088265; http://dx.doi.org/10.1074/mcp.M600335-MCP200
   PubMed Web of Science ®Google Scholar
• Poon JS, Eves R, Mak AS. Both lipid- and protein-phosphatase activities of PTEN contribute to the p53-PTEN anti-invasion pathway. Cell Cycle 2010; 9:4450 - 4454; PMID: 21084866; http://dx.doi.org/10.4161/cc.9.22.13936
   PubMed Web of Science ®Google Scholar
• Liang J, Slingerland JM. Multiple roles of the PI3K/PKB (Akt) pathway in cell cycle progression. Cell Cycle 2003; 2:339 - 345; PMID: 12851486; http://dx.doi.org/10.4161/cc.2.4.433
   PubMed Web of Science ®Google Scholar
• Héron-Milhavet L, Franckhauser C, Rana V, Berthenet C, Fisher D, Hemmings BA, et al. Only Akt1 is required for proliferation, while Akt2 promotes cell cycle exit through p21 binding. Mol Cell Biol 2006; 26:8267 - 8280; PMID: 16982699; http://dx.doi.org/10.1128/MCB.00201-06
   PubMed Web of Science ®Google Scholar
• Yun SJ, Tucker DF, Kim EK, Kim MS, Do KH, Ha JM, et al. Differential regulation of Akt/protein kinase B isoforms during cell cycle progression. FEBS Lett 2009; 583:685 - 690; PMID: 19166849; http://dx.doi.org/10.1016/j.febslet.2009.01.005
   PubMed Web of Science ®Google Scholar
• Shackelford RE, Kaufmann WK, Paules RS. Oxidative stress and cell cycle checkpoint function. Free Radic Biol Med 2000; 28:1387 - 1404; PMID: 10924858; http://dx.doi.org/10.1016/S0891-5849(00)00224-0
   PubMed Web of Science ®Google Scholar
• Shin JS, Hong SW, Lee SL, Kim TH, Park IC, An SK, et al. Serum starvation induces G1 arrest through suppression of Skp2-CDK2 and CDK4 in SK-OV-3 cells. Int J Oncol 2008; 32:435 - 439; PMID: 18202766
   PubMed Web of Science ®Google Scholar
• Sen CK, Roy S. Redox signals in wound healing. Biochim Biophys Acta 2008; 1780:1348 - 1361
   PubMed Web of Science ®Google Scholar
• Roy S, Khanna S, Nallu K, Hunt TK, Sen CK. Dermal wound healing is subject to redox control. Mol Ther 2006; 13:211 - 220; PMID: 16126008; http://dx.doi.org/10.1016/j.ymthe.2005.07.684
   PubMed Web of Science ®Google Scholar
• Steiling H, Munz B, Werner S, Brauchle M. Different types of ROS-scavenging enzymes are expressed during cutaneous wound repair. Exp Cell Res 1999; 247:484 - 494; PMID: 10066376; http://dx.doi.org/10.1006/excr.1998.4366
   PubMed Web of Science ®Google Scholar
• Héron-Milhavet L, Mamaeva D, Rochat A, Lamb NJ, Fernandez A. Akt2 is implicated in skeletal muscle differentiation and specifically binds Prohibitin2/REA. J Cell Physiol 2008; 214:158 - 165; PMID: 17565718; http://dx.doi.org/10.1002/jcp.21177
   PubMed Web of Science ®Google Scholar
• Ardite E, Barbera JA, Roca J, Fernandez-Checa JC. Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NFkappaB activation. Am J Pathol 2004; 165:719 - 728; PMID: 15331397; http://dx.doi.org/10.1016/S0002-9440(10)63335-4
   PubMed Web of Science ®Google Scholar
• Hansen JM, Klass M, Harris C, Csete M. A reducing redox environment promotes C2C12 myogenesis: implications for regeneration in aged muscle. Cell Biol Int 2007; 31:546 - 553; PMID: 17241791; http://dx.doi.org/10.1016/j.cellbi.2006.11.027
   PubMed Web of Science ®Google Scholar
• Lyons CN, Leary SC, Moyes CD. Bioenergetic remodeling during cellular differentiation: changes in cytochrome c oxidase regulation do not affect the metabolic phenotype. Biochem Cell Biol 2004; 82:391 - 399; PMID: 15181473; http://dx.doi.org/10.1139/o04-040
   PubMed Web of Science ®Google Scholar
• Muslin AJ. Akt2: a critical regulator of cardiomyocyte survival and metabolism. Pediatr Cardiol 2011; 32:317 - 322; PMID: 21279637; http://dx.doi.org/10.1007/s00246-010-9879-2
   PubMed Web of Science ®Google Scholar
• DeBosch B, Sambandam N, Weinheimer C, Courtois M, Muslin AJ. Akt2 regulates cardiac metabolism and cardiomyocyte survival. J Biol Chem 2006; 281:32841 - 32851; PMID: 16950770; http://dx.doi.org/10.1074/jbc.M513087200
   PubMed Web of Science ®Google Scholar
• Robin E, Guzy RD, Loor G, Iwase H, Waypa GB, Marks JD, et al. Oxidant stress during simulated ischemia primes cardiomyocytes for cell death during reperfusion. J Biol Chem 2007; 282:19133 - 19143; PMID: 17488710; http://dx.doi.org/10.1074/jbc.M701917200
   PubMed Web of Science ®Google Scholar
• Ceriello A, Motz E. Is oxidative stress the pathogenic mechanism underlying insulin resistance, diabetes and cardiovascular disease? The common soil hypothesis revisited. Arterioscler Thromb Vasc Biol 2004; 24:816 - 823; PMID: 14976002; http://dx.doi.org/10.1161/01.ATV.0000122852.22604.78
   PubMed Web of Science ®Google Scholar
• Maritim AC, Sanders RA, Watkins JB 3rd. Diabetes, oxidative stress and antioxidants: a review. J Biochem Mol Toxicol 2003; 17:24 - 38; PMID: 12616644; http://dx.doi.org/10.1002/jbt.10058
   PubMed Web of Science ®Google Scholar
• Brozinick JT Jr, Roberts BR, Dohm GL. Defective signaling through Akt-2 and -3 but not Akt-1 in insulin-resistant human skeletal muscle: potential role in insulin resistance. Diabetes 2003; 52:935 - 941; PMID: 12663464; http://dx.doi.org/10.2337/diabetes.52.4.935
   PubMed Web of Science ®Google Scholar
• Cho H, Mu J, Kim JK, Thorvaldsen JL, Chu Q, Crenshaw EB 3rd, et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 2001; 292:1728 - 1731; PMID: 11387480; http://dx.doi.org/10.1126/science.292.5522.1728
   PubMed Web of Science ®Google Scholar
• Dummler B, Hemmings BA. Physiological roles of PKB/Akt isoforms in development and disease. Biochem Soc Trans 2007; 35:231 - 235; PMID: 17371246; http://dx.doi.org/10.1042/BST0350231
   PubMed Web of Science ®Google Scholar
• George S, Rochford JJ, Wolfrum C, Gray SL, Schinner S, Wilson JC, et al. A family with severe insulin resistance and diabetes due to a mutation in AKT2. Science 2004; 304:1325 - 1328; PMID: 15166380; http://dx.doi.org/10.1126/science.1096706
   PubMed Web of Science ®Google Scholar