The function of the microtubule-associated protein tau is variably modulated by graded changes in glycogen synthase kinase-3β activity

被引:28
作者
Leroy, K
Menu, R
Conreur, JL
Dayanandan, R
Lovestone, S
Anderton, BH
Brion, JP
机构
[1] Free Univ Brussels, Sch Med, Lab Pathol & Electron Microscopy, B-1070 Brussels, Belgium
[2] Inst Psychiat, Dept Neurosci, London SE5 8AF, England
基金
英国惠康基金;
关键词
tau; glycogen synthase kinase-3 beta; microtubule; cell process; phosphorylation; lithium;
D O I
10.1016/S0014-5793(99)01720-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The microtubule-associated protein tau favors microtubule nucleation and stabilization and plays a role in the elongation of axons. We have investigated the ability of glycogen synthase kinase-3 beta (GSK-3 beta) to control tau-induced processes outgrowth. Tau-transfected Chinese hamster ovary (CHO) cells developed processes containing microtubule bundles after cytochalasin treatment, but a significant reduction in the number of cells harboring processes was observed in tau/GSK-3 beta-cotransfected cells. Lithium, an inhibitor of GSK-3 beta, counteracted in a dose-dependent manner this inhibitory effect of GSK-3 beta. These findings suggest that GSK-3 beta modulates in a graded manner the ability of tau to control. the microtubule-dependent induction of cell processes. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:34 / 38
页数:5
相关论文
共 25 条
[1]   The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains [J].
Biernat, J ;
Mandelkow, EM .
MOLECULAR BIOLOGY OF THE CELL, 1999, 10 (03) :727-740
[2]   ABNORMAL TAU-PHOSPHORYLATION AT SER(396) IN ALZHEIMERS-DISEASE RECAPITULATES DEVELOPMENT AND CONTRIBUTES TO REDUCED MICROTUBULE-BINDING [J].
BRAMBLETT, GT ;
GOEDERT, M ;
JAKES, R ;
MERRICK, SE ;
TROJANOWSKI, JQ ;
LEE, VMY .
NEURON, 1993, 10 (06) :1089-1099
[3]   TAU IN ALZHEIMER NEUROFIBRILLARY TANGLES - N-TERMINAL AND C-TERMINAL REGIONS ARE DIFFERENTIALLY ASSOCIATED WITH PAIRED HELICAL FILAMENTS AND THE LOCATION OF A PUTATIVE ABNORMAL PHOSPHORYLATION SITE [J].
BRION, JP ;
HANGER, DP ;
BRUCE, MT ;
COUCK, AM ;
FLAMENTDURAND, J ;
ANDERTON, BH .
BIOCHEMICAL JOURNAL, 1991, 273 :127-133
[4]   AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease [J].
BueeScherrer, V ;
Condamines, O ;
MourtonGilles, C ;
Jakes, R ;
Goedert, M ;
Pau, B ;
Delacourte, A .
MOLECULAR BRAIN RESEARCH, 1996, 39 (1-2) :79-88
[5]   INHIBITION OF NEURITE POLARITY BY TAU ANTISENSE OLIGONUCLEOTIDES IN PRIMARY CEREBELLAR NEURONS [J].
CACERES, A ;
KOSIK, KS .
NATURE, 1990, 343 (6257) :461-463
[6]  
DEGARCINI EM, 1994, MOL CELL BIOCHEM, V130, P187
[7]  
Delacourte A, 1997, INT REV CYTOL, V171, P167
[8]  
EDSON K, 1993, DEVELOPMENT, V117, P689
[9]   EPITOPE MAPPING OF MONOCLONAL-ANTIBODIES TO THE PAIRED HELICAL FILAMENTS OF ALZHEIMERS-DISEASE - IDENTIFICATION OF PHOSPHORYLATION SITES IN TAU-PROTEIN [J].
GOEDERT, M ;
JAKES, R ;
CROWTHER, RA ;
COHEN, P ;
VANMECHELEN, E ;
VANDERMEEREN, M ;
CRAS, P .
BIOCHEMICAL JOURNAL, 1994, 301 :871-877
[10]   Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3 [J].
Hong, M ;
Chen, DCR ;
Klein, PS ;
Lee, VMY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (40) :25326-25332