Efficient formation of bipolar microtubule bundles requires microtubule-bound γ-tubulin complexes

被引:108
作者
Janson, ME [1 ]
Setty, TG
Paoletti, A
Tran, PT
机构
[1] Univ Penn, Philadelphia, PA 19104 USA
[2] Inst Curie, CNRS, UMR 144, F-75231 Paris, France
关键词
D O I
10.1083/jcb.200410119
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The mechanism for forming linear microtubule (MT) arrays in cells such as neurons, polarized epithelial cells, and myotubes is not well understood. A simpler bipolar linear array is the fission yeast interphase MT bundle, which in its basic form contains two MTs that are bundled at their minus ends. Here, we characterize mto2p as a novel fission yeast protein required for MT nucleation from noncentrosomal gamma-tubulin complexes (gamma-TuCs). In interphase mto2 Delta cells, MT nucleation was strongly inhibited, and MT bundling occurred infrequently and only when two MTs met by chance in the cytoplasm. In wild-type 2, we observed MT nucleation from gamma-TuCs bound along the length of existing MTs. We propose a model on how these nucleation events can more efficiently drive the formation of bipolar MT bundles in interphase. Key to the model is our observation of selective antiparallel binding of MTs, which can both explain the generation and spatial separation of multiple bipolar bundles.
引用
收藏
页码:297 / 308
页数:12
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