THE ALZHEIMER-LIKE PHOSPHORYLATION OF TAU-PROTEIN REDUCES MICROTUBULE BINDING AND INVOLVES SER-PRO AND THR-PRO MOTIFS

被引:181
作者
GUSTKE, N
STEINER, B
MANDELKOW, EM
BIERNAT, J
MEYER, HE
GOEDERT, M
MANDELKOW, E
机构
[1] DESY, MAX PLANCK UNIT STRUCT MOLEC BIOL, NOTKESTR 85, W-2000 HAMBURG 52, GERMANY
[2] RUHR UNIV BOCHUM, INST PHYSIOL CHEM, W-4630 BOCHUM, GERMANY
[3] MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND
来源
FEBS LETTERS | 1992年 / 307卷 / 02期
关键词
TAU-PROTEIN; MICROTUBULE; ALZHEIMERS DISEASE; PHOSPHORYLATION; PROLINE-DIRECTED KINASE;
D O I
10.1016/0014-5793(92)80767-B
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
Tau protein can be transformed into an Alzheimer-like state by phosphorylation with a kinase activity from brain [Biernat et al. (1992) EMBO J. 11, 1593-1597]. Here we show that the phosphorylation at Ser-Pro motifs strongly decreases tau's affinity for microtubules. The major reduction occurs during the first of the three main stages of phosphorylation. The data explain the lower stability of microtubules resulting from the pathological tau phosphorylation.
引用
收藏
页码:199 / 205
页数:7
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