메뉴 건너뛰기




Volumn 591, Issue 7, 2017, Pages 1053-1063

C-terminal truncation of GSK-3β enhances its dephosphorylation by PP2A

Author keywords

Alzheimer's disease; glycogen synthase kinase 3 ; phosphorylation; protein phosphatase 2A; truncation

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; PHOSPHOPROTEIN PHOSPHATASE 2A; SERINE; PHOSPHOPROTEIN PHOSPHATASE 2; PROTEIN BINDING;

EID: 85016475088     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12617     Document Type: Article
Times cited : (9)

References (45)
  • 2
    • 0025904444 scopus 로고
    • A68: a major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee VM, Balin BJ, Otvos L Jr and Trojanowski JQ (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 251, 675–678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 3
  • 4
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso AC, Grundke-Iqbal I and Iqbal K (1996) Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 2, 783–787.
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 5
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso AC, Zaidi T, Grundke-Iqbal I and Iqbal K (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci USA 91, 5562–5566.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 6
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso A, Zaidi T, Novak M, Grundke-Iqbal I and Iqbal K (2001) Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci USA 98, 6923–6928.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 7
    • 0023200370 scopus 로고
    • Histopathological criteria for progressive dementia disorders: clinical-pathological correlation and classification by multivariate data analysis
    • Alafuzoff I, Iqbal K, Friden H, Adolfsson R and Winblad B (1987) Histopathological criteria for progressive dementia disorders: clinical-pathological correlation and classification by multivariate data analysis. Acta Neuropathol 74, 209–225.
    • (1987) Acta Neuropathol , vol.74 , pp. 209-225
    • Alafuzoff, I.1    Iqbal, K.2    Friden, H.3    Adolfsson, R.4    Winblad, B.5
  • 8
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada PV, Growdon JH, Hedley-Whyte ET and Hyman BT (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42, 631–639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 9
    • 0036224457 scopus 로고    scopus 로고
    • Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: findings from the Nun Study
    • Riley KP, Snowdon DA and Markesbery WR (2002) Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: findings from the Nun Study. Ann Neurol 51, 567–577.
    • (2002) Ann Neurol , vol.51 , pp. 567-577
    • Riley, K.P.1    Snowdon, D.A.2    Markesbery, W.R.3
  • 11
    • 0037163879 scopus 로고    scopus 로고
    • Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta
    • Liu F, Iqbal K, Grundke-Iqbal I and Gong CX (2002) Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. FEBS Lett 530, 209–214.
    • (2002) FEBS Lett , vol.530 , pp. 209-214
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Gong, C.X.4
  • 12
    • 0034731461 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice
    • Spittaels K, Van den Haute C, Van Dorpe J, Geerts H, Mercken M, Bruynseels K, Lasrado R, Vandezande K, Laenen I, Boon T et al. (2000) Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J Biol Chem 275, 41340–41349.
    • (2000) J Biol Chem , vol.275 , pp. 41340-41349
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3    Geerts, H.4    Mercken, M.5    Bruynseels, K.6    Lasrado, R.7    Vandezande, K.8    Laenen, I.9    Boon, T.10
  • 13
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R and Avila J (2001) Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J 20, 27–39.
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 14
    • 33746210131 scopus 로고    scopus 로고
    • Cooexpression of FTDP-17 tau and GSK-3beta in transgenic mice induce tau polymerization and neurodegeneration
    • Engel T, Lucas JJ, Gomez-Ramos P, Moran MA, Avila J and Hernandez F (2006) Cooexpression of FTDP-17 tau and GSK-3beta in transgenic mice induce tau polymerization and neurodegeneration. Neurobiol Aging 27, 1258–1268.
    • (2006) Neurobiol Aging , vol.27 , pp. 1258-1268
    • Engel, T.1    Lucas, J.J.2    Gomez-Ramos, P.3    Moran, M.A.4    Avila, J.5    Hernandez, F.6
  • 15
    • 0242720372 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model
    • Perez M, Hernandez F, Lim F, Diaz-Nido J and Avila J (2003) Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J Alzheimers Dis 5, 301–308.
    • (2003) J Alzheimers Dis , vol.5 , pp. 301-308
    • Perez, M.1    Hernandez, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 18
    • 65949119740 scopus 로고    scopus 로고
    • Calpain-mediated truncation of GSK-3 in post-mortem brain samples
    • Goni-Oliver P, Avila J and Hernandez F (2009) Calpain-mediated truncation of GSK-3 in post-mortem brain samples. J Neurosci Res 87, 1156–1161.
    • (2009) J Neurosci Res , vol.87 , pp. 1156-1161
    • Goni-Oliver, P.1    Avila, J.2    Hernandez, F.3
  • 19
    • 84952718143 scopus 로고    scopus 로고
    • Truncation and activation of GSK-3β by calpain I: a molecular mechanism links to tau hyperphosphorylation in Alzheimer's disease
    • Jin N, Yin X, Yu D, Cao M, Gong CX, Iqbal K, Ding F, Gu X and Liu F (2015) Truncation and activation of GSK-3β by calpain I: a molecular mechanism links to tau hyperphosphorylation in Alzheimer's disease. Sci Rep 5, 8187.
    • (2015) Sci Rep , vol.5 , pp. 8187
    • Jin, N.1    Yin, X.2    Yu, D.3    Cao, M.4    Gong, C.X.5    Iqbal, K.6    Ding, F.7    Gu, X.8    Liu, F.9
  • 20
    • 34547929974 scopus 로고    scopus 로고
    • N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation
    • Goni-Oliver P, Lucas JJ, Avila J and Hernandez F (2007) N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation. J Biol Chem 282, 22406–22413.
    • (2007) J Biol Chem , vol.282 , pp. 22406-22413
    • Goni-Oliver, P.1    Lucas, J.J.2    Avila, J.3    Hernandez, F.4
  • 21
    • 84863305898 scopus 로고    scopus 로고
    • Site-specific phosphorylation protects glycogen synthase kinase-3β from calpain-mediated truncation of its N and C termini
    • Ma S, Liu S, Huang Q, Xie B, Lai B, Wang C, Song B and Li M (2012) Site-specific phosphorylation protects glycogen synthase kinase-3β from calpain-mediated truncation of its N and C termini. J Biol Chem 287, 22521–22532.
    • (2012) J Biol Chem , vol.287 , pp. 22521-22532
    • Ma, S.1    Liu, S.2    Huang, Q.3    Xie, B.4    Lai, B.5    Wang, C.6    Song, B.7    Li, M.8
  • 22
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling
    • Sutherland C, Leighton IA and Cohen P (1993) Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem J 296 (Pt 1), 15–19.
    • (1993) Biochem J , vol.296 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 23
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang QM, Fiol CJ, DePaoli-Roach AA and Roach PJ (1994) Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J Biol Chem 269, 14566–14574.
    • (1994) J Biol Chem , vol.269 , pp. 14566-14574
    • Wang, Q.M.1    Fiol, C.J.2    DePaoli-Roach, A.A.3    Roach, P.J.4
  • 24
    • 0032557646 scopus 로고    scopus 로고
    • Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB
    • van Weeren PC, de Bruyn KM, de Vries-Smits AM, van Lint J and Burgering BM (1998) Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J Biol Chem 273, 13150–13156.
    • (1998) J Biol Chem , vol.273 , pp. 13150-13156
    • van Weeren, P.C.1    de Bruyn, K.M.2    de Vries-Smits, A.M.3    van Lint, J.4    Burgering, B.M.5
  • 25
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M and Hemmings BA (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785–789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 26
    • 84948703497 scopus 로고    scopus 로고
    • GSK-3beta is dephosphorylated by PP2A in a Leu309 methylation-independent manner
    • Chu D, Tan J, Xie S, Jin N, Yin X, Gong CX, Iqbal K and Liu F (2015) GSK-3beta is dephosphorylated by PP2A in a Leu309 methylation-independent manner. J Alzheimers Dis 49, 365–375.
    • (2015) J Alzheimers Dis , vol.49 , pp. 365-375
    • Chu, D.1    Tan, J.2    Xie, S.3    Jin, N.4    Yin, X.5    Gong, C.X.6    Iqbal, K.7    Liu, F.8
  • 30
    • 0028897322 scopus 로고
    • Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases
    • Singh TJ, Zaidi T, Grundke-Iqbal I and Iqbal K (1995) Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS Lett 358, 4–8.
    • (1995) FEBS Lett , vol.358 , pp. 4-8
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 31
    • 33750510335 scopus 로고    scopus 로고
    • PKA modulates GSK-3beta- and cdk5-catalyzed phosphorylation of tau in site- and kinase-specific manners
    • Liu F, Liang Z, Shi J, Yin D, El-Akkad E, Grundke-Iqbal I, Iqbal K and Gong CX (2006) PKA modulates GSK-3beta- and cdk5-catalyzed phosphorylation of tau in site- and kinase-specific manners. FEBS Lett 580, 6269–6274.
    • (2006) FEBS Lett , vol.580 , pp. 6269-6274
    • Liu, F.1    Liang, Z.2    Shi, J.3    Yin, D.4    El-Akkad, E.5    Grundke-Iqbal, I.6    Iqbal, K.7    Gong, C.X.8
  • 32
    • 19244367909 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimer's disease
    • Hernandez F, Perez M, Lucas JJ, Mata AM, Bhat R and Avila J (2004) Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimer's disease. J Biol Chem 279, 3801–3806.
    • (2004) J Biol Chem , vol.279 , pp. 3801-3806
    • Hernandez, F.1    Perez, M.2    Lucas, J.J.3    Mata, A.M.4    Bhat, R.5    Avila, J.6
  • 34
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D and Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519–526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 35
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik KS, Orecchio LD, Bakalis S and Neve RL (1989) Developmentally regulated expression of specific tau sequences. Neuron 2, 1389–1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 36
    • 65249116483 scopus 로고    scopus 로고
    • Tau mutations in neurodegenerative diseases
    • Wolfe MS (2009) Tau mutations in neurodegenerative diseases. J Biol Chem 284, 6021–6025.
    • (2009) J Biol Chem , vol.284 , pp. 6021-6025
    • Wolfe, M.S.1
  • 37
    • 26444581827 scopus 로고    scopus 로고
    • Tau gene mutations and their effects
    • Goedert M (2005) Tau gene mutations and their effects. Mov Disord 20 (Suppl 12), S45–S52.
    • (2005) Mov Disord , vol.20 , pp. S45-S52
    • Goedert, M.1
  • 38
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • Liu F and Gong CX (2008) Tau exon 10 alternative splicing and tauopathies. Mol Neurodegener 3, 8.
    • (2008) Mol Neurodegener , vol.3 , pp. 8
    • Liu, F.1    Gong, C.X.2
  • 39
    • 77950366745 scopus 로고    scopus 로고
    • PP2A regulates tau phosphorylation directly and also indirectly via activating GSK-3beta
    • Qian W, Shi J, Yin X, Iqbal K, Grundke-Iqbal I, Gong CX and Liu F (2010) PP2A regulates tau phosphorylation directly and also indirectly via activating GSK-3beta. J Alzheimers Dis 19, 1221–1229.
    • (2010) J Alzheimers Dis , vol.19 , pp. 1221-1229
    • Qian, W.1    Shi, J.2    Yin, X.3    Iqbal, K.4    Grundke-Iqbal, I.5    Gong, C.X.6    Liu, F.7
  • 40
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • Liu F, Grundke-Iqbal I, Iqbal K and Gong CX (2005) Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci 22, 1942–1950.
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 41
    • 79960343311 scopus 로고    scopus 로고
    • Calpain regulates N-terminal interaction of GSK-3beta with 14-3-3zeta, p53 and PKB but not with axin
    • Goni-Oliver P, Avila J and Hernandez F (2011) Calpain regulates N-terminal interaction of GSK-3beta with 14-3-3zeta, p53 and PKB but not with axin. Neurochem Int 59, 97–100.
    • (2011) Neurochem Int , vol.59 , pp. 97-100
    • Goni-Oliver, P.1    Avila, J.2    Hernandez, F.3
  • 43
    • 84856583036 scopus 로고    scopus 로고
    • Calpain in the CNS: from synaptic function to neurotoxicity
    • Liu J, Liu MC and Wang KK (2008) Calpain in the CNS: from synaptic function to neurotoxicity. Sci Signal 1, re1.
    • (2008) Sci Signal , vol.1 , pp. re1
    • Liu, J.1    Liu, M.C.2    Wang, K.K.3
  • 44
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278–84
    • Braak H and Braak E (1995) Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol Aging 16, 271–278; discussion 278–84.
    • (1995) Neurobiol Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 45
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G and Berg L (1991) The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 41, 479–486.
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    van Belle, G.9    Berg, L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.