메뉴 건너뛰기




Volumn 7, Issue 23, 2008, Pages 3699-3708

A mitotic role for GSK-3β kinase in Drosophila

Author keywords

Drosophila; GSK 3 ; Mitosis; sgg; Zw3

Indexed keywords

DROSOPHILA PROTEIN; GLYCOGEN SYNTHASE KINASE 3BETA; PROTEIN ZW3; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 57349122327     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.23.7179     Document Type: Article
Times cited : (8)

References (38)
  • 1
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • Jope RS, Johnson GV. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci 2004; 29:95-102.
    • (2004) Trends Biochem Sci , vol.29 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.2
  • 2
    • 18244377210 scopus 로고    scopus 로고
    • Wnt/beta-catenin pathway
    • Moon RT. Wnt/beta-catenin pathway. Sci STKE 2005; 2005:1.
    • (2005) Sci STKE 2005 , pp. 1
    • Moon, R.T.1
  • 3
    • 0025241896 scopus 로고
    • Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates
    • Fiol CJ, Wang A, Roeske RW, Roach PJ. Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates. J Biol Chem 1990; 265:6061-5.
    • (1990) J Biol Chem , vol.265 , pp. 6061-6065
    • Fiol, C.J.1    Wang, A.2    Roeske, R.W.3    Roach, P.J.4
  • 4
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly PJ, Krebs EG. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 1991; 266:15555-8.
    • (1991) J Biol Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 5
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors: Development and therapeutic potential
    • Cohen P, Goedert M. GSK3 inhibitors: development and therapeutic potential. Nat Rev Drug Discov 2004; 3:479-87.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 6
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussel MF, Sherr CJ. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 1998; 12:3499-511.
    • (1998) Genes Dev , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 8
    • 0037442990 scopus 로고    scopus 로고
    • A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment
    • Wakefield JG, Stephens DJ, Tavaré JM. A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment. J Cell Sci 2003; 116:637-46.
    • (2003) J Cell Sci , vol.116 , pp. 637-646
    • Wakefield, J.G.1    Stephens, D.J.2    Tavaré, J.M.3
  • 9
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351:95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 10
    • 4344619713 scopus 로고    scopus 로고
    • Pharmacological inhibitors of glycogen synthase kinase 3
    • Meijer L, Flajolet M, Greengard P. Pharmacological inhibitors of glycogen synthase kinase 3. Trends Pharmacol Sci 2004; 25:471-80.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 471-480
    • Meijer, L.1    Flajolet, M.2    Greengard, P.3
  • 12
    • 36048983139 scopus 로고    scopus 로고
    • Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation
    • Selenica M-L, Jensen HS, Larsen AK, Pedersen ML, Helboe L, Leist M, Lotharius J. Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation. Br J Pharmacol 2007; 152:959-79.
    • (2007) Br J Pharmacol , vol.152 , pp. 959-979
    • Selenica, M.-L.1    Jensen, H.S.2    Larsen, A.K.3    Pedersen, M.L.4    Helboe, L.5    Leist, M.6    Lotharius, J.7
  • 14
    • 30044442183 scopus 로고    scopus 로고
    • Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb
    • Smelkinson MG, Kalderon D. Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb. Curr Biol 2006; 16:110-6.
    • (2006) Curr Biol , vol.16 , pp. 110-116
    • Smelkinson, M.G.1    Kalderon, D.2
  • 15
  • 16
    • 0034699332 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase protein slimb regulates centrosome duplication in Drosophila
    • Wojcik EJ, Glover DM, Hays TS. The SCF ubiquitin ligase protein slimb regulates centrosome duplication in Drosophila. Curr Biol 2000; 10:1131-4.
    • (2000) Curr Biol , vol.10 , pp. 1131-1134
    • Wojcik, E.J.1    Glover, D.M.2    Hays, T.S.3
  • 17
    • 33646871571 scopus 로고    scopus 로고
    • Shaggy/GSK-3beta kinase localizes to the centrosome and to specialized cytoskeletal structures in Drosophila
    • Bobinnec Y, Morin X, Debec A. Shaggy/GSK-3beta kinase localizes to the centrosome and to specialized cytoskeletal structures in Drosophila. Cell Motil Cytoskeleton 2006; 63:313-20.
    • (2006) Cell Motil Cytoskeleton , vol.63 , pp. 313-320
    • Bobinnec, Y.1    Morin, X.2    Debec, A.3
  • 18
    • 0028047389 scopus 로고
    • wingless signal and Zeste-white 3 kinase trigger opposing changes in the intracellular distribution of Armadillo
    • Peifer M, Sweeton D, Casey M, Wieschaus E. wingless signal and Zeste-white 3 kinase trigger opposing changes in the intracellular distribution of Armadillo. Development 1994; 120:369-80.
    • (1994) Development , vol.120 , pp. 369-380
    • Peifer, M.1    Sweeton, D.2    Casey, M.3    Wieschaus, E.4
  • 20
    • 0028217346 scopus 로고
    • Determinants of Drosophila zw10 protein localization and function
    • Williams BC, Goldberg ML. Determinants of Drosophila zw10 protein localization and function. J Cell Sci 1994; 107:785-98.
    • (1994) J Cell Sci , vol.107 , pp. 785-798
    • Williams, B.C.1    Goldberg, M.L.2
  • 21
    • 45149086638 scopus 로고    scopus 로고
    • GSK-3beta regulates proper mitotic spindle formation in cooperation with a component of the gamma-tubulin ring complex, GCP5
    • Izumi N, Fumoto K, Izumi S, Kikuchi A. GSK-3beta regulates proper mitotic spindle formation in cooperation with a component of the gamma-tubulin ring complex, GCP5. J Biol Chem 2008; 283:12981-91.
    • (2008) J Biol Chem , vol.283 , pp. 12981-12991
    • Izumi, N.1    Fumoto, K.2    Izumi, S.3    Kikuchi, A.4
  • 22
    • 0142060928 scopus 로고    scopus 로고
    • Thienyl and phenyl alpha-halomethyl ketones: New inhibitors of glycogen synthase kinase (GSK-3beta) from a library of compound searching
    • Conde S, Pérez DI, Martínez A, Perez C, Moreno FJ. Thienyl and phenyl alpha-halomethyl ketones: new inhibitors of glycogen synthase kinase (GSK-3beta) from a library of compound searching. J Med Chem 2003; 46:4631-3.
    • (2003) J Med Chem , vol.46 , pp. 4631-4633
    • Conde, S.1    Pérez, D.I.2    Martínez, A.3    Perez, C.4    Moreno, F.J.5
  • 23
    • 28544449332 scopus 로고    scopus 로고
    • SAR and 3D-QSAR studies on thiadiazolidinone derivatives: Exploration of structural requirements for glycogen synthase kinase 3 inhibitors
    • Martinez A, Alonso M, Castro A, Dorronsoro I, Gelpí JL, Luque FJ, Pérez C, Moreno FJ. SAR and 3D-QSAR studies on thiadiazolidinone derivatives: exploration of structural requirements for glycogen synthase kinase 3 inhibitors. J Med Chem 2005; 48:7103-12.
    • (2005) J Med Chem , vol.48 , pp. 7103-7112
    • Martinez, A.1    Alonso, M.2    Castro, A.3    Dorronsoro, I.4    Gelpí, J.L.5    Luque, F.J.6    Pérez, C.7    Moreno, F.J.8
  • 24
    • 0035211977 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B phosphorylation by glycogen synthase kinase 3beta is induced during PC12 cell differentiation
    • Goold RG, Gordon-Weeks PR. Microtubule-associated protein 1B phosphorylation by glycogen synthase kinase 3beta is induced during PC12 cell differentiation. J Cell Sci 2001; 114:4273-84.
    • (2001) J Cell Sci , vol.114 , pp. 4273-4284
    • Goold, R.G.1    Gordon-Weeks, P.R.2
  • 25
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S, Hartley CL, Pearce J, Anderton BH. Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience 1996; 73:1145-57.
    • (1996) Neuroscience , vol.73 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Anderton, B.H.4
  • 26
    • 0028981873 scopus 로고
    • Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells
    • Sperber BR, Leight S, Goedert M, Lee VM. Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells. Neurosci Lett 1995; 197:149-53.
    • (1995) Neurosci Lett , vol.197 , pp. 149-153
    • Sperber, B.R.1    Leight, S.2    Goedert, M.3    Lee, V.M.4
  • 27
    • 0035176077 scopus 로고    scopus 로고
    • Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation
    • Zumbrunn J, Kinoshita K, Hyman AA, Näthke IS. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Curr Biol 2001; 11:44-9.
    • (2001) Curr Biol , vol.11 , pp. 44-49
    • Zumbrunn, J.1    Kinoshita, K.2    Hyman, A.A.3    Näthke, I.S.4
  • 30
    • 0242664588 scopus 로고    scopus 로고
    • Structural Insights and Biological Effects of Glycogen Synthase Kinase 3-specific Inhibitor AR-A014418
    • Bhat R. Structural Insights and Biological Effects of Glycogen Synthase Kinase 3-specific Inhibitor AR-A014418. J Biol Chem 2003; 278:45937-45.
    • (2003) J Biol Chem , vol.278 , pp. 45937-45945
    • Bhat, R.1
  • 31
    • 0032705583 scopus 로고    scopus 로고
    • The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity
    • Hers I, Tavaré JM, Denton RM. The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity. FEBS Lett 1999; 460:433-6.
    • (1999) FEBS Lett , vol.460 , pp. 433-436
    • Hers, I.1    Tavaré, J.M.2    Denton, R.M.3
  • 32
    • 0035153295 scopus 로고    scopus 로고
    • Microtubule-dependent changes in assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at PtK1 kinetochores
    • Hoffman DB, Pearson CG, Yen TJ, Howell BJ, Salmon ED. Microtubule-dependent changes in assembly of microtubule motor proteins and mitotic spindle checkpoint proteins at PtK1 kinetochores. Mol Biol Cell 2001; 12:1995-2009.
    • (2001) Mol Biol Cell , vol.12 , pp. 1995-2009
    • Hoffman, D.B.1    Pearson, C.G.2    Yen, T.J.3    Howell, B.J.4    Salmon, E.D.5
  • 33
    • 0033578025 scopus 로고    scopus 로고
    • Mad2 binding by phosphorylated kinetochores links error detection and checkpoint action in mitosis
    • Waters JC, Chen RH, Murray AW, Gorbsky GJ, Salmon ED, Nicklas RB. Mad2 binding by phosphorylated kinetochores links error detection and checkpoint action in mitosis. Curr Biol 1999; 9:649-52.
    • (1999) Curr Biol , vol.9 , pp. 649-652
    • Waters, J.C.1    Chen, R.H.2    Murray, A.W.3    Gorbsky, G.J.4    Salmon, E.D.5    Nicklas, R.B.6
  • 34
    • 0027070855 scopus 로고
    • wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate
    • Siegfried E, Chou TB, Perrimon N. wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate. Cell 1992; 71:1167-79.
    • (1992) Cell , vol.71 , pp. 1167-1179
    • Siegfried, E.1    Chou, T.B.2    Perrimon, N.3
  • 35
    • 0035910097 scopus 로고    scopus 로고
    • A protein trap strategy to detect GFP-tagged proteins expressed from their endogenous loci in Drosophila
    • Morin X, Daneman R, Zavortink M, Chia W. A protein trap strategy to detect GFP-tagged proteins expressed from their endogenous loci in Drosophila. Proc Natl Acad Sci USA 2001; 98:15050-5.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15050-15055
    • Morin, X.1    Daneman, R.2    Zavortink, M.3    Chia, W.4
  • 36
    • 0242385551 scopus 로고    scopus 로고
    • Flattening Drosophila cells for high-resolution light microscopic studies of mitosis in vitro
    • Fleming SL, Rieder CL. Flattening Drosophila cells for high-resolution light microscopic studies of mitosis in vitro. Cell Motil Cytoskeleton 2003; 56:141-6.
    • (2003) Cell Motil Cytoskeleton , vol.56 , pp. 141-146
    • Fleming, S.L.1    Rieder, C.L.2
  • 37
    • 0035736325 scopus 로고    scopus 로고
    • Kinetochore dynein: Its dynamics and role in the transport of the Rough deal checkpoint protein
    • Wojcik E, Basto R, Serr M, Scaërou F, Karess R, Hays T. Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein. Nat Cell Biol 2001; 3:1001-7.
    • (2001) Nat Cell Biol , vol.3 , pp. 1001-1007
    • Wojcik, E.1    Basto, R.2    Serr, M.3    Scaërou, F.4    Karess, R.5    Hays, T.6
  • 38
    • 85011937999 scopus 로고    scopus 로고
    • Rasband WS. ImageJ. US National Institutes of Health, Bethesda, MD USA
    • Rasband WS. ImageJ. US National Institutes of Health, Bethesda, MD USA.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.