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Published online 18 April 2005. doi:10.1083/jcb.200410119
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 2, 297-308
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Article

 Efficient formation of bipolar microtubule bundles requires microtubule-bound {gamma}-tubulin complexes

Marcel E. Janson1, Thanuja Gangi Setty1, Anne Paoletti2, and P.T. Tran1

1 Cell and Developmental Biology, University of Pennsylvania, Philadelphia, PA 19104
2 Institut Curie, UMR 144 CNRS, Paris, France

Correspondence to Marcel E. Janson: mjanson{at}mail.med.upenn.edu; or P.T. Tran: tranp{at}mail.med.upenn.edu

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.

Abbreviations used in this paper: MBC, methyl-benzidazole-carbamate; MT, microtubule; mRFP, monomeric RFP; MTOC, MT organizing center; DIC, differential interference contrast; SPB, spindle pole body; iMTOC, interphase MTOC; eMTOC, equatorial MTOC; {gamma}-TuC, {gamma}-tubulin complex.


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