期刊
SCIENCE
卷 363, 期 6424, 页码 285-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aav2567
关键词
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资金
- ERC [StG 715289]
- Swiss National Science Foundation (SNSF) [PP00P3_157517]
- University of Geneva
- Czech Science Foundation [18-08304S]
- project BIOCEV from the ERDF [CZ.1.05/1.1.00/02.0109]
- CAS [RVO: 86652036]
- GAUK [1372218]
- MEYS CR (Czech-BioImaging) [LM2015062]
Microtubule doublets (MTDs), consisting of an incomplete B-microtubule at the surface of a complete A-microtubule, provide a structural scaffold mediating intraflagellar transport and ciliary beating. Despite the fundamental role of MTDs, the molecular mechanism governing their formation is unknown. We used a cell-free assay to demonstrate a crucial inhibitory role of the carboxyl-terminal (C-terminal) tail of tubulin in MTD assembly. Removal of the C-terminal tail of an assembled A-microtubule allowed for the nucleation of a B-microtubule on its surface. C-terminal tails of only one A-microtubule protofilament inhibited this side-to-surface tubulin interaction, which would be overcome in vivo with binding protein partners. The dynamics of B-microtubule nucleation and its distinctive isotropic elongation was elucidated by using live imaging. Thus, inherent interaction properties of tubulin provide a structural basis driving flagellar MTD assembly.
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