메뉴 건너뛰기




Volumn 154, Issue 2, 1996, Pages 143-151

Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain

Author keywords

Alzheimer disease; GSK 3; Microtubules; Paired helical filaments; Protein kinases; Tau protein

Indexed keywords

CASEIN KINASE I; CYCLIC AMP DEPENDENT PROTEIN KINASE; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN KINASE C; TAU PROTEIN;

EID: 0030067749     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00226782     Document Type: Article
Times cited : (42)

References (26)
  • 1
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G, Cole RD: Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem 259: 5301-5305, 1984
    • (1984) J Biol Chem , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 2
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11: 153-163, 1993
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 9
    • 0026784416 scopus 로고
    • P42 map kinase phosphorylation sites in microtubule-associated protein tau are dephos-phorylated by protein phosphatase 2A
    • Goedert M, Cohen ES, Jakes R, Cohen P: P42 map kinase phosphorylation sites in microtubule-associated protein tau are dephos-phorylated by protein phosphatase 2A. FEBS Lett 312: 95-99, 1992
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 12
    • 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: Abnormal Alzheimer-like phosphorylation of tau protein by cyclin dependent kinases cdk2 and cdk5. FEBS Lett 336: 417-424, 1993
    • (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
  • 13
    • 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: 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: 23512-23518, 1993
    • (1993) J Biol Chem , vol.268 , pp. 23512-23518
    • Paudel, H.K.1    Lew, J.2    Ali, Z.3    Wang, J.H.4
  • 15
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3β is identical to tau protein kinase I, generating several epitopes of paired helical filaments
    • Ishiguro K, Shiratsuchi A, Sato S, Omori A, Arioka M, Kobayashi S, Uchida T, Imahori K: Glycogen synthase kinase 3β is identical to tau protein kinase I, generating several epitopes of paired helical filaments. FEBS Lett 325: 167-172, 1993
    • (1993) FEBS Lett , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3    Omori, A.4    Arioka, M.5    Kobayashi, S.6    Uchida, T.7    Imahori, K.8
  • 16
    • 0027340541 scopus 로고
    • A/GSK-3 phosphorylates τ on ser 235-pro and ser 404-pro that are abnormally phosphorylated in Alzheimer's disease brain
    • A/GSK-3 phosphorylates τ on ser 235-pro and ser 404-pro that are abnormally phosphorylated in Alzheimer's disease brain. J Neurochem 61: 1742-1747, 1993
    • (1993) J Neurochem , vol.61 , pp. 1742-1747
    • Yang, S.-D.1    Song, J.-S.2    Yu, J.-S.3    Shiah, S.-G.4
  • 17
    • 0028967378 scopus 로고
    • Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3
    • Singh TJ, Haque N, Grundke-Iqbal I, Iqbal K: Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3. FEBS Lett 358: 267-272, 1995
    • (1995) FEBS Lett , vol.358 , pp. 267-272
    • Singh, T.J.1    Haque, N.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 18
    • 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, Iqbal K: Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS Lett 358: 4-8, 1995
    • (1995) FEBS Lett , vol.358 , pp. 4-8
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 19
    • 0026597280 scopus 로고
    • Phosphorylation of cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky JM, Johnson GVW: Phosphorylation of cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J Biol Chem 267: 1563-1568, 1992
    • (1992) J Biol Chem , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.W.2
  • 21
    • 0028871109 scopus 로고
    • Phosphorylation of tau protein by casein kinase-1 converts it to an abnormal Alzheimer-like state
    • Singh TJ, Grundke-Iqbal I, Iqbal K: Phosphorylation of tau protein by casein kinase-1 converts it to an abnormal Alzheimer-like state. J Neurochem 64: 1420-1423, 1995
    • (1995) J Neurochem , vol.64 , pp. 1420-1423
    • Singh, T.J.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 22
    • 0023624478 scopus 로고
    • Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by calcium/phospholipid-dependent protein kinase
    • Baudier J, Lee S-H, Cole RD: Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by calcium/phospholipid-dependent protein kinase. J Biol Chem 262: 17584-17590, 1987
    • (1987) J Biol Chem , vol.262 , pp. 17584-17590
    • Baudier, J.1    Lee, S.-H.2    Cole, R.D.3
  • 23
    • 0026625670 scopus 로고
    • Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin-binding domain
    • Correas I, Diaz-Nido J, Avila J: Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin-binding domain. J Biol Chem 267: 15721-15728, 1992
    • (1992) J Biol Chem , vol.267 , pp. 15721-15728
    • Correas, I.1    Diaz-Nido, J.2    Avila, J.3
  • 24
    • 0023630392 scopus 로고
    • Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by calcium/calmodulin-dependent protein kinase and modulated by phospholipids
    • Baudier J, Cole RD: Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by calcium/calmodulin-dependent protein kinase and modulated by phospholipids. J Biol Chem 262: 17577-17583, 1991
    • (1991) J Biol Chem , vol.262 , pp. 17577-17583
    • Baudier, J.1    Cole, R.D.2
  • 25
    • 0028220180 scopus 로고
    • Comparison of the phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases
    • Singh TJ, Grundke-Iqbal I, McDonald B, Iqbal K: Comparison of the phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. Mol Cell Biochem 131: 181-189, 1994
    • (1994) Mol Cell Biochem , vol.131 , pp. 181-189
    • Singh, T.J.1    Grundke-Iqbal, I.2    McDonald, B.3    Iqbal, K.4
  • 26
    • 0028049937 scopus 로고
    • Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert
    • Greenwood JA, Scott CW, Spreen RC, Caputo CB, Johnson GVW: Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. J Biol Chem 269: 4373-4380, 1994
    • (1994) J Biol Chem , vol.269 , pp. 4373-4380
    • Greenwood, J.A.1    Scott, C.W.2    Spreen, R.C.3    Caputo, C.B.4    Johnson, G.V.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.