메뉴 건너뛰기




Volumn 107, Issue 7, 2010, Pages 2884-2889

No difference in kinetics of tau or histone phosphorylation by CDK5/p25 versus CDK5/p35 in vitro

Author keywords

Alzheimer's disease; Neurotoxicity; NMR; Protein kinase; Proteolysis

Indexed keywords

CALPAIN; CYCLIN DEPENDENT KINASE 5; HISTONE H1; PROTEIN P25; PROTEIN P35; TAU PROTEIN;

EID: 77649250664     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0912718107     Document Type: Article
Times cited : (46)

References (54)
  • 1
    • 0025856776 scopus 로고
    • A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope
    • Ishiguro K, et al. (1991) A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope. Neurosci Lett 128:195-8.
    • (1991) Neurosci Lett , vol.128 , pp. 195-198
    • Ishiguro, K.1
  • 2
    • 0026731425 scopus 로고
    • Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments
    • Ishiguro K, et al. (1992) Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. J Biol Chem 267:10897-901.
    • (1992) J Biol Chem , vol.267 , pp. 10897-10901
    • Ishiguro, K.1
  • 3
    • 0026680802 scopus 로고
    • Purification and characterization of a novel proline-directed protein kinase from bovine brain
    • Lew J, Beaudette K, Litwin CM, Wang JH (1992) Purification and characterization of a novel proline-directed protein kinase from bovine brain. J Biol Chem 267:13383-90.
    • (1992) J Biol Chem , vol.267 , pp. 13383-13390
    • Lew, J.1    Beaudette, K.2    Litwin, C.M.3    Wang, J.H.4
  • 4
    • 0027087170 scopus 로고
    • Brain proline-directed protein kinase is a neurofilament kinase which displays high sequence homology to p34cdc2
    • Lew J, Winkfein RJ, Paudel HK, Wang JH (1992) Brain proline-directed protein kinase is a neurofilament kinase which displays high sequence homology to p34cdc2. J Biol Chem 267:25922-6.
    • (1992) J Biol Chem , vol.267 , pp. 25922-25926
    • Lew, J.1    Winkfein, R.J.2    Paudel, H.K.3    Wang, J.H.4
  • 5
  • 6
    • 0028207389 scopus 로고
    • Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain
    • Ishiguro K, et al. (1994) Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain. FEBS Lett 342:203-8.
    • (1994) FEBS Lett , vol.342 , pp. 203-208
    • Ishiguro, K.1
  • 7
    • 0028122011 scopus 로고
    • A brain-specific activator of cyclin-dependent kinase
    • Lew J, et al. (1994) A brain-specific activator of cyclin-dependent kinase. Nature 371:423-6.
    • (1994) Nature , vol.371 , pp. 423-426
    • Lew, J.1
  • 8
    • 0027978170 scopus 로고
    • p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5
    • Tsai LH, Delalle I, Caviness VS, Jr, Chae T, Harlow E (1994) p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5. Nature 371:419-23.
    • (1994) Nature , vol.371 , pp. 419-423
    • Tsai, L.H.1    Delalle, I.2    Caviness Jr, V.S.3    Chae, T.4    Harlow, E.5
  • 9
    • 0027971397 scopus 로고
    • Precursor of cdk5 activator, the 23 kDa subunit of tau protein kinase II: Its sequence and developmental change in brain
    • Uchida T, et al. (1994) Precursor of cdk5 activator, the 23 kDa subunit of tau protein kinase II: its sequence and developmental change in brain. FEBS Lett 355:35-40.
    • (1994) FEBS Lett , vol.355 , pp. 35-40
    • Uchida, T.1
  • 10
    • 2942572871 scopus 로고    scopus 로고
    • A Jekyll and Hyde kinase: Roles for Cdk5 in brain development and disease
    • Cruz JC, Tsai LH (2004) A Jekyll and Hyde kinase: roles for Cdk5 in brain development and disease. Curr Opin Neurobiol 14:390-4.
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 390-394
    • Cruz, J.C.1    Tsai, L.H.2
  • 11
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick GN, et al. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402:615-22.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1
  • 12
    • 0035951413 scopus 로고    scopus 로고
    • Calpain-mediated degradation of p35 to p25 in postmortem human and rat brains
    • Taniguchi S, et al. (2001) Calpain-mediated degradation of p35 to p25 in postmortem human and rat brains. FEBS Lett 489:46-50.
    • (2001) FEBS Lett , vol.489 , pp. 46-50
    • Taniguchi, S.1
  • 13
    • 0035933621 scopus 로고    scopus 로고
    • Involvement of cyclin dependent kinase5 activator p25 on tau phosphorylation in mouse brain
    • Takashima A, et al. (2001) Involvement of cyclin dependent kinase5 activator p25 on tau phosphorylation in mouse brain. Neurosci Lett 306:37-40.
    • (2001) Neurosci Lett , vol.306 , pp. 37-40
    • Takashima, A.1
  • 15
    • 0035859053 scopus 로고    scopus 로고
    • p25 protein in neurodegeneration
    • discussion 764-5
    • Yoo BC, Lubec G (2001) p25 protein in neurodegeneration. Nature 411:763-4 discussion 764-5.
    • (2001) Nature , vol.411 , pp. 763-764
    • Yoo, B.C.1    Lubec, G.2
  • 16
    • 0041803010 scopus 로고    scopus 로고
    • Brain levels of CDK5 activator p25 are not increased in Alzheimer's or other neurodegenerative diseases with neurofibrillary tangles
    • Tandon A, et al. (2003) Brain levels of CDK5 activator p25 are not increased in Alzheimer's or other neurodegenerative diseases with neurofibrillary tangles. J Neurochem 86:572-81.
    • (2003) J Neurochem , vol.86 , pp. 572-581
    • Tandon, A.1
  • 17
    • 0037125209 scopus 로고    scopus 로고
    • A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains
    • Tseng HC, Zhou Y, Shen Y, Tsai LH (2002) A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains. FEBS Lett 523:58-62.
    • (2002) FEBS Lett , vol.523 , pp. 58-62
    • Tseng, H.C.1    Zhou, Y.2    Shen, Y.3    Tsai, L.H.4
  • 18
    • 0036771832 scopus 로고    scopus 로고
    • AbetaPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576
    • Otth C, et al. (2002) AbetaPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576. J Alzheimers Dis 4:417-30.
    • (2002) J Alzheimers Dis , vol.4 , pp. 417-430
    • Otth, C.1
  • 19
    • 0344823864 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model of Parkinson's disease
    • Smith PD, et al. (2003) Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model of Parkinson's disease. P Natl Acad Sci USA 100:13650-5.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 13650-13655
    • Smith, P.D.1
  • 20
    • 17744368458 scopus 로고    scopus 로고
    • Deregulation of Cdk5 in a mouse model of ALS: Toxicity alleviated by perikaryal neurofilament inclusions
    • Nguyen MD, Lariviere RC, Julien JP (2001) Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron 30:135-47.
    • (2001) Neuron , vol.30 , pp. 135-147
    • Nguyen, M.D.1    Lariviere, R.C.2    Julien, J.P.3
  • 21
    • 0031446275 scopus 로고    scopus 로고
    • Association of cyclin-dependent kinase 5 and its activator p35 with apoptotic cell death
    • Ahuja HS, Zhu Y, Zakeri Z (1997) Association of cyclin-dependent kinase 5 and its activator p35 with apoptotic cell death. Dev Genet 21:258-67.
    • (1997) Dev Genet , vol.21 , pp. 258-267
    • Ahuja, H.S.1    Zhu, Y.2    Zakeri, Z.3
  • 22
    • 0036312755 scopus 로고    scopus 로고
    • Cdk5 phosphorylates p53 and regulates its activity
    • Zhang J, Krishnamurthy PK, Johnson GV (2002) Cdk5 phosphorylates p53 and regulates its activity. J Neurochem 81:307-13.
    • (2002) J Neurochem , vol.81 , pp. 307-313
    • Zhang, J.1    Krishnamurthy, P.K.2    Johnson, G.V.3
  • 23
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee MS, et al. (2000) Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 405:360-4.
    • (2000) Nature , vol.405 , pp. 360-364
    • Lee, M.S.1
  • 24
    • 0032508698 scopus 로고    scopus 로고
    • p35: The neuronalspecific activator of cyclin-dependent kinase 5 (Cdk5) is degraded by the ubiquitinproteasome pathway
    • Patrick GN, Zhou P, Kwon YT, Howley PM, Tsai LH (1998) p35: the neuronalspecific activator of cyclin-dependent kinase 5 (Cdk5) is degraded by the ubiquitinproteasome pathway. J Biol Chem 273:24057-64.
    • (1998) J Biol Chem , vol.273 , pp. 24057-24064
    • Patrick, G.N.1    Zhou, P.2    Kwon, Y.T.3    Howley, P.M.4    Tsai, L.H.5
  • 25
    • 0036434290 scopus 로고    scopus 로고
    • Cleavage of the cyclin-dependent kinase 5 activator p35 to p25 does not induce tau hyperphosphorylation
    • Kerokoski P, Suuronen T, Salminen A, Soininen H, Pirttila T (2002) Cleavage of the cyclin-dependent kinase 5 activator p35 to p25 does not induce tau hyperphosphorylation. Biochem Biophys Res Commun 298:693-8.
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 693-698
    • Kerokoski, P.1    Suuronen, T.2    Salminen, A.3    Soininen, H.4    Pirttila, T.5
  • 26
    • 0347785492 scopus 로고    scopus 로고
    • Truncation of CDK5 activator p35 induces intensive phosphorylation of Ser202/Thr205 of human tau
    • Hashiguchi M, Saito T, Hisanaga S, Hashiguchi T (2002) Truncation of CDK5 activator p35 induces intensive phosphorylation of Ser202/Thr205 of human tau. J Biol Chem 277:44525-30.
    • (2002) J Biol Chem , vol.277 , pp. 44525-44530
    • Hashiguchi, M.1    Saito, T.2    Hisanaga, S.3    Hashiguchi, T.4
  • 27
    • 0027485937 scopus 로고
    • Substrate specificity characterization of a cdc2-like protein kinase purified from bovine brain
    • Beaudette KN, Lew J, Wang JH (1993) Substrate specificity characterization of a cdc2-like protein kinase purified from bovine brain. J Biol Chem 268:20825-30.
    • (1993) J Biol Chem , vol.268 , pp. 20825-20830
    • Beaudette, K.N.1    Lew, J.2    Wang, J.H.3
  • 28
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K, Mandelkow EM, Biernat J, Piwnica-Worms H, Mandelkow E (1993) Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett 336:417-24.
    • (1993) FEBS Lett , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 29
    • 0029618170 scopus 로고
    • Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites
    • Ishiguro K, et al. (1995) Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites. Neurosci Lett 202:81-4.
    • (1995) Neurosci Lett , vol.202 , pp. 81-84
    • Ishiguro, K.1
  • 30
    • 0027421625 scopus 로고
    • Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments
    • Paudel HK, Lew J, Ali Z, Wang JH (1993) Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments. J Biol Chem 268:23512-8.
    • (1993) J Biol Chem , vol.268 , pp. 23512-23518
    • Paudel, H.K.1    Lew, J.2    Ali, Z.3    Wang, J.H.4
  • 31
    • 0035109902 scopus 로고    scopus 로고
    • Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry
    • Lund ET, McKenna R, Evans DB, Sharma SK, Mathews WR (2001) Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry. J Neurochem 76:1221-32.
    • (2001) J Neurochem , vol.76 , pp. 1221-1232
    • Lund, E.T.1    McKenna, R.2    Evans, D.B.3    Sharma, S.K.4    Mathews, W.R.5
  • 32
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimer's disease
    • Illenberger S, et al. (1998) The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol Biol Cell 9:1495-512.
    • (1998) Mol Biol Cell , vol.9 , pp. 1495-1512
    • Illenberger, S.1
  • 33
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
    • Hasegawa M, et al. (1992) Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. J Biol Chem 267:17047-54.
    • (1992) J Biol Chem , vol.267 , pp. 17047-17054
    • Hasegawa, M.1
  • 34
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (1998) New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J Neurochem 71:2465-76.
    • (1998) J Neurochem , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3    Blackstock, W.P.4    Anderton, B.H.5
  • 35
    • 0028899714 scopus 로고
    • Proline-directed and non-proline-directed phosphorylation of PHF-tau
    • Morishima-Kawashima M, et al. (1995) Proline-directed and non-proline-directed phosphorylation of PHF-tau. J Biol Chem 270:823-9.
    • (1995) J Biol Chem , vol.270 , pp. 823-829
    • Morishima-Kawashima, M.1
  • 36
    • 34548191034 scopus 로고    scopus 로고
    • Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis
    • Hanger DP, et al. (2007) Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem 282:23645-54.
    • (2007) J Biol Chem , vol.282 , pp. 23645-23654
    • Hanger, D.P.1
  • 37
    • 0027370141 scopus 로고
    • In vivo phosphorylation sites in fetal and adult rat tau
    • Watanabe A, et al. (1993) In vivo phosphorylation sites in fetal and adult rat tau. J Biol Chem 268:25712-7.
    • (1993) J Biol Chem , vol.268 , pp. 25712-25717
    • Watanabe, A.1
  • 38
    • 49449101644 scopus 로고    scopus 로고
    • Kinetic studies of Cdk5/p25 kinase: Phosphorylation of tau and complex inhibition by two prototype inhibitors
    • Liu M, et al. (2008) Kinetic studies of Cdk5/p25 kinase: phosphorylation of tau and complex inhibition by two prototype inhibitors. Biochemistry 47:8367-77.
    • (2008) Biochemistry , vol.47 , pp. 8367-8377
    • Liu, M.1
  • 39
    • 22544457646 scopus 로고    scopus 로고
    • Defining Cdk5 ligand chemical space with small molecule inhibitors of tau phosphorylation
    • Ahn JS, et al. (2005) Defining Cdk5 ligand chemical space with small molecule inhibitors of tau phosphorylation. Chem Biol 12:811-23.
    • (2005) Chem Biol , vol.12 , pp. 811-823
    • Ahn, J.S.1
  • 40
    • 0031965914 scopus 로고    scopus 로고
    • Possible role of tau protein kinases in pathogenesis of Alzheimer's disease
    • Imahori K, et al. (1998) Possible role of tau protein kinases in pathogenesis of Alzheimer's disease. Neurobiol Aging 19:S93-8.
    • (1998) Neurobiol Aging , vol.19
    • Imahori, K.1
  • 42
    • 12944268979 scopus 로고    scopus 로고
    • Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5
    • Ahlijanian MK, et al. (2000) Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5. Proc Natl Acad Sci USA 97:2910-5.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2910-2915
    • Ahlijanian, M.K.1
  • 43
    • 0037417767 scopus 로고    scopus 로고
    • MAP kinases and CDKs: Kinetic basis for catalytic activation
    • Lew J (2003) MAP kinases and CDKs: kinetic basis for catalytic activation. Biochemistry 42:849-56.
    • (2003) Biochemistry , vol.42 , pp. 849-856
    • Lew, J.1
  • 44
    • 65349143103 scopus 로고    scopus 로고
    • Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules
    • Amniai L, et al. (2009) Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules. Faseb J 23:1146-52.
    • (2009) Faseb J , vol.23 , pp. 1146-1152
    • Amniai, L.1
  • 45
    • 0347065362 scopus 로고    scopus 로고
    • Substrate specificity of CDK2-cyclin A. What is optimal?
    • Stevenson-Lindert LM, Fowler P, Lew J (2003) Substrate specificity of CDK2-cyclin A. What is optimal?. J Biol Chem 278:50956-60.
    • (2003) J Biol Chem , vol.278 , pp. 50956-50960
    • Stevenson-Lindert, L.M.1    Fowler, P.2    Lew, J.3
  • 46
    • 0034595834 scopus 로고    scopus 로고
    • Calpain-dependent proteolytic cleavage of the p35 cyclindependent kinase 5 activator to p25
    • Kusakawa G, et al. (2000) Calpain-dependent proteolytic cleavage of the p35 cyclindependent kinase 5 activator to p25. J Biol Chem 275:17166-72.
    • (2000) J Biol Chem , vol.275 , pp. 17166-17172
    • Kusakawa, G.1
  • 47
    • 24744462506 scopus 로고    scopus 로고
    • Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39
    • Sakaue F, et al. (2005) Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39. J Biol Chem 280:31522-9.
    • (2005) J Biol Chem , vol.280 , pp. 31522-31529
    • Sakaue, F.1
  • 49
    • 0033710860 scopus 로고    scopus 로고
    • Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth
    • Zukerberg LR, et al. (2000) Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth. Neuron 26:633-46.
    • (2000) Neuron , vol.26 , pp. 633-646
    • Zukerberg, L.R.1
  • 50
    • 47249159078 scopus 로고    scopus 로고
    • A soluble oligomer of tau associated with fiber formation analyzed by NMR
    • Peterson DW, Zhou H, Dahlquist FW, Lew J (2008) A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry 47:7393-404.
    • (2008) Biochemistry , vol.47 , pp. 7393-7404
    • Peterson, D.W.1    Zhou, H.2    Dahlquist, F.W.3    Lew, J.4
  • 51
    • 0034705010 scopus 로고    scopus 로고
    • Catalytic reaction pathway for the mitogen-activated protein kinase ERK2
    • Prowse CN, Hagopian JC, Cobb MH, Ahn NG, Lew J (2000) Catalytic reaction pathway for the mitogen-activated protein kinase ERK2. Biochemistry 39:6258-66.
    • (2000) Biochemistry , vol.39 , pp. 6258-6266
    • Prowse, C.N.1    Hagopian, J.C.2    Cobb, M.H.3    Ahn, N.G.4    Lew, J.5
  • 52
    • 0029400480 scopus 로고
    • nmrPipe-a Multidimensional Spectral Processing System Based On Unix Pipes
    • Delaglio F, et al. (1995) nmrPipe-a Multidimensional Spectral Processing System Based On Unix Pipes. J Biomol NMR 6:277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 53
    • 0001250026 scopus 로고
    • ANSIG: A Program for the Assignment of Protein 1H 2D NMR spectra by Interactive Graphics
    • Kraulis PJ (1989) ANSIG: A Program for the Assignment of Protein 1H 2D NMR spectra by Interactive Graphics. J Magn Reson 24:627-633.
    • (1989) J Magn Reson , vol.24 , pp. 627-633
    • Kraulis, P.J.1
  • 54
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED (1994) Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry 33:3515-31.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.