Identification of Rictor as a Novel Substrate of Polo-like kinase 1

References

• Gruneberg U, Neef R, Honda R, Nigg EA, Barr FA. Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2. J Cell Biol 2004; 166:167-72; PMID:15263015; http://dx.doi.org/10.1083/jcb.200403084
   PubMed Web of Science ®Google Scholar
• Strebhardt K. Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy. Nat Rev Drug Discov 2010; 9:643-60; PMID:20671765; http://dx.doi.org/10.1038/nrd3184
   PubMed Web of Science ®Google Scholar
• van de Weerdt BC, Medema RH. Polo-like kinases: a team in control of the division. Cell Cycle 2006; 5:853-64; PMID:16627997; http://dx.doi.org/10.4161/cc.5.8.2692
   PubMed Web of Science ®Google Scholar
• Yim H, Erikson RL. Polo-like kinase 1 depletion induces DNA damage in early S prior to caspase activation. Mol Cell Biol 2009; 29:2609-21; PMID:19289504; http://dx.doi.org/10.1128/MCB.01277-08
   PubMed Web of Science ®Google Scholar
• Trenz K, Errico A, Costanzo V. Plx1 is required for chromosomal DNA replication under stressful conditions. Embo J 2008; 27:876-85; PMID:18309293; http://dx.doi.org/10.1038/emboj.2008.29
   PubMed Web of Science ®Google Scholar
• Lei M, Erikson RL. Plk1 depletion in nontransformed diploid cells activates the DNA-damage checkpoint. Oncogene 2008; 27:3935-43; PMID:18297112; http://dx.doi.org/10.1038/onc.2008.36
   PubMed Web of Science ®Google Scholar
• Song B, Liu XS, Davis K, Liu X. Plk1 phosphorylation of Orc2 promotes DNA replication under conditions of stress. Mol Cell Biol 2011; 31:4844-56; PMID:21947279; http://dx.doi.org/10.1128/MCB.06110-11
   PubMed Web of Science ®Google Scholar
• Keppner S, Proschak E, Schneider G, Spankuch B. Fate of primary cells at the G(1)/S boundary after polo-like kinase 1 inhibition by SBE13. Cell Cycle 2011; 10:708-20; PMID:21301227; http://dx.doi.org/10.4161/cc.10.4.14898
   PubMed Web of Science ®Google Scholar
• Liu X, Erikson RL. Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc Natl Acad Sci U S A 2003; 100:5789-94; PMID:12732729; http://dx.doi.org/10.1073/pnas.1031523100
   PubMed Web of Science ®Google Scholar
• Tamura Y, Simizu S, Muroi M, Takagi S, Kawatani M, Watanabe N, Osada H. Polo-like kinase 1 phosphorylates and regulates Bcl-x(L) during pironetin-induced apoptosis. Oncogene 2009; 28:107-16; PMID:18820703; http://dx.doi.org/10.1038/onc.2008.368
   PubMed Web of Science ®Google Scholar
• Liu X, Lei M, Erikson RL. Normal cells, but not cancer cells, survive severe Plk1 depletion. Mol Cell Biol 2006; 26:2093-108; PMID:16507989; http://dx.doi.org/10.1128/MCB.26.6.2093-2108.2006
   PubMed Web of Science ®Google Scholar
• Keppner S, Proschak E, Kaufmann M, Strebhardt K, Schneider G, Spankuch B. Biological impact of freezing Plk1 in its inactive conformation in cancer cells. Cell Cycle 2010; 9:761-73; PMID:20139717; http://dx.doi.org/10.4161/cc.9.4.10644
   PubMed Web of Science ®Google Scholar
• Lu LY, Wood JL, Minter-Dykhouse K, Ye L, Saunders TL, Yu X, Chen J. Polo-like kinase 1 is essential for early embryonic development and tumor suppression. Mol Cell Biol 2008; 28:6870-6; PMID:18794363; http://dx.doi.org/10.1128/MCB.00392-08
   PubMed Web of Science ®Google Scholar
• Renner AG, Creancier L, Dos Santos C, Fialin C, Recher C, Bailly C, Kruczynski A, Payrastre B, Manenti S. A functional link between polo-like kinase 1 and the mammalian target-of-rapamycin pathway? Cell Cycle 2010; 9:1690-6; PMID:20404504; http://dx.doi.org/10.4161/cc.9.9.11295
   PubMed Web of Science ®Google Scholar
• Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, Tokunaga C, Avruch J, Yonezawa K. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 2002; 110:177-89; PMID:12150926; http://dx.doi.org/10.1016/S0092-8674(02)00833-4
   PubMed Web of Science ®Google Scholar
• Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 2002; 110:163-75; PMID:12150925; http://dx.doi.org/10.1016/S0092-8674(02)00808-5
   PubMed Web of Science ®Google Scholar
• Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004; 14:1296-302; PMID:15268862; http://dx.doi.org/10.1016/j.cub.2004.06.054
   PubMed Web of Science ®Google Scholar
• Zoncu R, Efeyan A, Sabatini DM. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 2011; 12 :21-35; PMID:21157483; http://dx.doi.org/10.1038/nrm3025
   PubMed Web of Science ®Google Scholar
• Ma XM, Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat Rev Mol Cell Biol 2009; 10:307-18; PMID:19339977; http://dx.doi.org/10.1038/nrm2672
   PubMed Web of Science ®Google Scholar
• Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, Bonenfant D, Oppliger W, Jenoe P, Hall MN. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell 2002; 10:457-68; PMID:12408816; http://dx.doi.org/10.1016/S1097-2765(02)00636-6
   PubMed Web of Science ®Google Scholar
• Jacinto E, Loewith R, Schmidt A, Lin S, Ruegg MA, Hall A, Hall MN. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol 2004; 6:1122-8; PMID:15467718; http://dx.doi.org/10.1038/ncb1183
   PubMed Web of Science ®Google Scholar
• Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005; 307:1098-101; PMID:15718470; http://dx.doi.org/10.1126/science.1106148
   PubMed Web of Science ®Google Scholar
• Facchinetti V, Ouyang W, Wei H, Soto N, Lazorchak A, Gould C, Lowry C, Newton AC, Mao Y, Miao RQ, et al. The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. Embo J 2008; 27:1932-43; PMID:18566586; http://dx.doi.org/10.1038/emboj.2008.120
   PubMed Web of Science ®Google Scholar
• Ikenoue T, Inoki K, Yang Q, Zhou X, Guan KL. Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling. Embo J 2008; 27:1919-31; PMID:18566587; http://dx.doi.org/10.1038/emboj.2008.119
   PubMed Web of Science ®Google Scholar
• Iliuk A, Liu XS, Xue L, Liu X, Tao WA. Chemical visualization of phosphoproteomes on membrane. Mol Cell Proteomics 2012; 11:629-39; PMID:22593177; http://dx.doi.org/10.1074/mcp.O112.018010
   PubMed Web of Science ®Google Scholar
• Jacinto E, Facchinetti V, Liu D, Soto N, Wei S, Jung SY, Huang Q, Qin J, Su B. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 2006; 127:125-37; PMID:16962653; http://dx.doi.org/10.1016/j.cell.2006.08.033
   PubMed Web of Science ®Google Scholar
• Yang CS, Song CH, Lee JS, Jung SB, Oh JH, Park J, Kim HJ, Park JK, Paik TH, Jo EK. Intracellular network of phosphatidylinositol 3-kinase, mammalian target of the rapamycin/70 kDa ribosomal S6 kinase 1, and mitogen-activated protein kinases pathways for regulating mycobacteria-induced IL-23 expression in human macrophages. Cell Microbiol 2006; 8:1158-71; PMID:16819968; http://dx.doi.org/10.1111/j.1462-5822.2006.00699.x
   PubMed Web of Science ®Google Scholar
• Strebhardt K, Ullrich A. Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 2006; 6:321-30; PMID:16557283; http://dx.doi.org/10.1038/nrc1841
   PubMed Web of Science ®Google Scholar
• Schmelzle T, Hall MN. TOR, a central controller of cell growth. Cell 2000; 103:253-62; PMID:11057898; http://dx.doi.org/10.1016/S0092-8674(00)00117-3
   PubMed Web of Science ®Google Scholar
• Gingras AC, Raught B, Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev 2001; 15:807-26; PMID:11297505; http://dx.doi.org/10.1101/gad.887201
   PubMed Web of Science ®Google Scholar
• Frias MA, Thoreen CC, Jaffe JD, Schroder W, Sculley T, Carr SA, Sabatini DM. mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. Curr Biol 2006; 16:1865-70; PMID:16919458; http://dx.doi.org/10.1016/j.cub.2006.08.001
   PubMed Web of Science ®Google Scholar
• Guertin DA, Stevens DM, Thoreen CC, Burds AA, Kalaany NY, Moffat J, Brown M, Fitzgerald KJ, Sabatini DM. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. Dev Cell 2006; 11:859-71; PMID:17141160; http://dx.doi.org/10.1016/j.devcel.2006.10.007
   PubMed Web of Science ®Google Scholar
• Blagosklonny MV. Cell cycle arrest is not yet senescence, which is not just cell cycle arrest: terminology for TOR-driven aging. Aging (Albany NY) 2012; 4:159-65; PMID:22394614
   PubMedGoogle Scholar
• Serrano M. Dissecting the role of mTOR complexes in cellular senescence. Cell Cycle 2012; 11:2231-2; PMID:22714590; http://dx.doi.org/10.4161/cc.21065
   PubMed Web of Science ®Google Scholar
• Khapre RV, Kondratova AA, Patel S, Dubrovsky Y, Wrobel M, Antoch MP, Kondratov RV. BMAL1-dependent regulation of the mTOR signaling pathway delays aging. Aging (Albany NY) 2014; 6:48-57; PMID:24481314
   PubMedGoogle Scholar