Regulation of Microtubule Assembly by Tau and not by Pin1
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- 作者：Steffen Kutter1 ; Timo Eichner1 ; 1 ; Alexandra M. Deaconescu1 ; 2 ; Dorothee Kern1 ; dkern@brandeis.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：MAP ; microtubule-associated protein ; MT ; microtubules ; SAXS ; small angle X-ray scattering ; EM ; electron microscopy ; FRET ; Fö ; rster resonance energy transfer ; EMBL ; European Molecular Biology Laboratory
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：8 May 2016
- 年：2016
- 卷：428
- 期：9
- 页码：1742-1759
- 全文大小：2787 K
文摘
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Novel GTP-tubulin rings are formed in the presence of tauSH and tau441.
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Tubulin rings may be on-pathway intermediates toward in vitro MT formation.
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Tau is bound to the outer surface of tubulin rings and MTs.
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Phosphorylation of T231 and/or Ser235 reduces the efficiency of tubulin polymerization.
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Pin1 cannot recover the ability of phosphorylated tau to induce tubulin polymerization.