10
Views
3
CrossRef citations to date
0
Altmetric
Article

Drosophila DBT Autophosphorylation of Its C-Terminal Domain Antagonized by SPAG and Involved in UV-Induced Apoptosis

, , &
Pages 2414-2424 | Received 14 Apr 2015, Accepted 28 Apr 2015, Published online: 20 Mar 2023

REFERENCES

  • Young MW, Kay SA. 2001. Time zones: a comparative genetics of circadian clocks. Nat Rev Genet 2:702–715. http://dx.doi.org/10.1038/35088576.
  • Takahashi JS, Hong HK, Ko CH, McDearmon EL. 2008. The genetics of mammalian circadian order and disorder: implications for physiology and disease. Nat Rev Genet 9:764–775. http://dx.doi.org/10.1038/nrg2430.
  • Hardin PE. 2011. Molecular genetic analysis of circadian timekeeping in Drosophila. Adv Genet 74:141–173. http://dx.doi.org/10.1016/B978-0-12-387690-4.00005-2.
  • Price JL, Blau J, Rothenfluh A, Abodeeley M, Kloss B, Young MW. 1998. Double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation. Cell 94:83–95. http://dx.doi.org/10.1016/S0092-8674(00)81224-6.
  • Muskus MJ, Preuss F, Fan JY, Bjes ES, Price JL. 2007. Drosophila DBT lacking protein kinase activity produces long-period and arrhythmic circadian behavioral and molecular rhythms. Mol Cell Biol 27:8049–8064. http://dx.doi.org/10.1128/MCB.00680-07.
  • Preuss F, Fan JY, Kalive M, Bao S, Schuenemann E, Bjes ES, Price JL. 2004. Drosophila doubletime mutations which either shorten or lengthen the period of circadian rhythms decrease the protein kinase activity of casein kinase. I Mol Cell Biol 24:886–898. http://dx.doi.org/10.1128/MCB.24.2.886-898.2004.
  • Kloss B, Price JL, Saez L, Blau J, Rothenfluh A, Wesley CS, Young MW. 1998. The Drosophila clock gene double-time encodes a protein closely related to human casein kinase Iε. Cell 94:97–107. http://dx.doi.org/10.1016/S0092-8674(00)81225-8.
  • Edery I, Zwiebel LJ, Dembinska ME, Rosbash M. 1994. Temporal phosphorylation of the Drosophila period protein. Proc Natl Acad Sci U S A 91:2260–2264. http://dx.doi.org/10.1073/pnas.91.6.2260.
  • Price JL, Dembinska ME, Young MW, Rosbash M. 1995. Suppression of PERIOD protein abundance and circadian cycling by the Drosophila clock mutation timeless. EMBO J 14:4044–4049.
  • Kloss B, Rothenfluh A, Young MW, Saez L. 2001. Phosphorylation of period is influenced by cycling physical associations of double-time, period, and timeless in the Drosophila clock. Neuron 30:699–706. http://dx.doi.org/10.1016/S0896-6273(01)00320-8.
  • Hunter-Ensor M, Ousley A, Sehgal A. 1996. Regulation of the Drosophila protein timeless suggests a mechanism for resetting the circadian clock by light. Cell 84:677–685. http://dx.doi.org/10.1016/S0092-8674(00)81046-6.
  • Myers MP, Wager-Smith K, Rothenfluh-Hilfiker A, Young MW. 1996. Light-induced degradation of TIMELESS and entrainment of the Drosophila circadian clock. Science 271:1736–1740. http://dx.doi.org/10.1126/science.271.5256.1736.
  • Zeng HK, Qian ZW, Myers MP, Rosbash M. 1996. A light-entrainment mechanism for the Drosophila circadian clock. Nature 380:129–135. http://dx.doi.org/10.1038/380129a0.
  • Rothenfluh A, Young MW, Saez L. 2000. A TIMELESS-independent function for PERIOD proteins in the Drosophila clock. Neuron 26:505–514. http://dx.doi.org/10.1016/S0896-6273(00)81182-4.
  • Fan JY, Agyekum B, Venkatesan A, Hall DR, Keightley A, Bjes ES, Bouyain S, Price JL. 2013. Noncanonical FK506-binding protein BDBT binds DBT to enhance its circadian function and forms foci at night. Neuron 80:984–996. http://dx.doi.org/10.1016/j.neuron.2013.08.004.
  • Graves PR, Roach PJ. 1995. Role of COOH-terminal phosphorylation in the regulation of casein kinase I delta. J Biol Chem 270:21689–21694. http://dx.doi.org/10.1074/jbc.270.37.21689.
  • Gietzen KF, Virshup DM. 1999. Identification of inhibitory autophosphorylation sites in casein kinase I epsilon. J Biol Chem 274:32063–32070. http://dx.doi.org/10.1074/jbc.274.45.32063.
  • Dahlberg CL, Nguyen EZ, Goodlett D, Kimelman D. 2009. Interactions between casein kinase Iepsilon (CKIepsilon) and two substrates from disparate signaling pathways reveal mechanisms for substrate-kinase specificity. PLoS One 4:e4766. http://dx.doi.org/10.1371/journal.pone.0004766.
  • Constance CM, Fan JY, Preuss F, Green CB, Price JL. 2005. The circadian clock-containing photoreceptor cells in Xenopus laevis express several isoforms of casein kinase I. Brain research. Mol Brain Res 136:199–211. http://dx.doi.org/10.1016/j.molbrainres.2005.02.009.
  • Lowrey PL, Shimomura K, Antoch MP, Yamazaki S, Zemenides PD, Ralph MR, Menaker M, Takahashi JS. 2000. Positional syntenic cloning and functional characterization of the mammalian circadian mutation tau. Science 288:483–492. http://dx.doi.org/10.1126/science.288.5465.483.
  • Fan JY, Preuss F, Muskus MJ, Bjes ES, Price JL. 2009. Drosophila and vertebrate casein kinase Idelta exhibits evolutionary conservation of circadian function. Genetics 181:139–152. http://dx.doi.org/10.1534/genetics.108.094805.
  • Guan J, Li H, Rogulja A, Axelrod JD, Cadigan KM. 2007. The Drosophila casein kinase Iepsilon/delta Discs overgrown promotes cell survival via activation of DIAP1 expression. Dev Biol 303:16–28. http://dx.doi.org/10.1016/j.ydbio.2006.10.028.
  • Means JC, Venkatesan A, Gerdes B, Fan JY, Bjes ES, Price JL. 2015. Drosophila Spaghetti and Doubletime link the circadian clock and light to caspases, apoptosis and tauopathy. PLoS Genet 11:e1005171. http://dx.doi.org/10.1371/journal.pgen.1005171.
  • Benbahouche Nel H, Iliopoulos I, Torok I, Marhold J, Henri J, Kajava AV, Farkas R, Kempf T, Schnolzer M, Meyer P, Kiss I, Bertrand E, Mechler BM, Pradet-Balade B. 2014. Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries. J Biol Chem 289:6236–6247. http://dx.doi.org/10.1074/jbc.M113.499608.
  • Keightley JA, Shang L, Kinter M. 2004. Proteomic analysis of oxidative stress-resistant cells: a specific role for aldose reductase overexpression in cytoprotection. Mol Cell Proteomics 3:167–175. http://dx.doi.org/10.1074/mcp.M300119-MCP200.
  • Price JL, Fan JY, Keightley A, Means JC. 2015. The role of casein kinase I in the Drosophila circadian clock. Methods Enzymol 551:175–195. http://dx.doi.org/10.1016/bs.mie.2014.10.012.
  • Bao S, Rihel J, Bjes E, Fan JY, Price JL. 2001. The Drosophila double-timeS mutation delays the nuclear accumulation of period protein and affects the feedback regulation of period mRNA. J Neurosci 21:7117–7126.
  • Zhai B, Villen J, Beausoleil SA, Mintseris J, Gygi SP. 2008. Phosphoproteome analysis of Drosophila melanogaster embryos. J Proteome Res 7:1675–1682. http://dx.doi.org/10.1021/pr700696a.
  • Bodenmiller B, Malmstrom J, Gerrits B, Campbell D, Lam H, Schmidt A, Rinner O, Mueller LN, Shannon PT, Pedrioli PG, Panse C, Lee HK, Schlapbach R, Aebersold R. 2007. PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Mol Systems Biol 3:139. http://dx.doi.org/10.1038/msb4100182.
  • Xu Y, Padiath QS, Shapiro RE, Jones CR, Wu SC, Saigoh N, Saigoh K, Ptacek LJ, Fu YH. 2005. Functional consequences of a CKIdelta mutation causing familial advanced sleep phase syndrome. Nature 434:640–644. http://dx.doi.org/10.1038/nature03453.
  • Yu W, Zheng H, Price JL, Hardin PE. 2009. DOUBLETIME plays a noncatalytic role to mediate CLOCK phosphorylation and repress CLOCK-dependent transcription within the Drosophila circadian clock. Mol Cell Biol 29:1452–1458. http://dx.doi.org/10.1128/MCB.01777-08.
  • Kim EY, Edery I. 2006. Balance between DBT/CKIepsilon kinase and protein phosphatase activities regulate phosphorylation and stability of Drosophila CLOCK protein. Proc Natl Acad Sci U S A 103:6178–6183. http://dx.doi.org/10.1073/pnas.0511215103.
  • Lowrey PL, Shimomura K, Antoch MP, Yamazaki S, Zemenides PD, Ralph MR, Menaker M, Takahashi JS. 2000. Positional syntenic cloning and functional characterization of the mammalian circadian mutation, tau. Science 288:483–491. http://dx.doi.org/10.1126/science.288.5465.483.
  • Suri V, Hall JC, Rosbash M. 2000. Two novel doubletime mutants alter circadian properties and eliminate the delay between RNA and protein in Drosophila. J Neurosci 20:7547–7555.
  • Eckert K, Saliou JM, Monlezun L, Vigouroux A, Atmane N, Caillat C, Quevillon-Cheruel S, Madiona K, Nicaise M, Lazereg S, Van Dorsselaer A, Sanglier-Cianferani S, Meyer P, Morera S. 2010. The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem 285:31304–31312. http://dx.doi.org/10.1074/jbc.M110.138263.
  • Boulon S, Marmier-Gourrier N, Pradet-Balade B, Wurth L, Verheggen C, Jady BE, Rothe B, Pescia C, Robert MC, Kiss T, Bardoni B, Krol A, Branlant C, Allmang C, Bertrand E, Charpentier B. 2008. The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery. J Cell Biol 180:579–595. http://dx.doi.org/10.1083/jcb.200708110.
  • Cheong JK, Nguyen TH, Wang H, Tan P, Voorhoeve PM, Lee SH, Virshup DM. 2011. IC261 induces cell cycle arrest and apoptosis of human cancer cells via CK1delta/varepsilon and Wnt/beta-catenin independent inhibition of mitotic spindle formation. Oncogene 30:2558–2569. http://dx.doi.org/10.1038/onc.2010.627.
  • Liu F, Virshup DM, Nairn AC, Greengard P. 2002. Mechanism of regulation of casein kinase I activity by group I metabotropic glutamate receptors. J Biol Chem 277:45393–45399. http://dx.doi.org/10.1074/jbc.M204499200.
  • Swiatek W, Tsai IC, Klimowski L, Pepler A, Barnette J, Yost HJ, Virshup DM. 2004. Regulation of casein kinase I epsilon activity by Wnt signaling. J Biol Chem 279:13011–13017. http://dx.doi.org/10.1074/jbc.M304682200.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.