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First published online November 19, 2008


Journal of Cell Science 121, 2305e (2008)
© The Company of Biologists Limited
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In this issue

Mto1/2 gets microtubules going


Figure 1

During nucleation – an essential early step in de novo formation of microtubules – the {gamma}-tubulin complex ({gamma}-TuC) is recruited to prospective microtubule-organising centres. Relatively little is known about how this occurs, although it is thought that – in fission yeast – the interacting proteins Mto1 and Mto2 recruit {gamma}-TuC. Ken Sawin and colleagues previously explored how knocking out mto1 or mto2 affected nucleation; now, on page 3971, they use site-directed mutagenesis of mto1 to further investigate the association of Mto1 and Mto2 with {gamma}-TuC. The authors first show that, similar to {Delta}mto1 mutants, cytoplasmic microtubule nucleation is abolished in fission yeast carrying a mutant mto1 with a disrupted centrosomin 1 motif (CM1) region; moreover, the mutant Mto1 does not interact with {gamma}-TuC, although it localises normally and interacts with Mto2. By contrast, mutations outside the CM1 region of Mto1 phenocopy {Delta}mto2 yeast – limited microtubule nucleation does occur, but binding of Mto1 to Mto2 or {gamma}-TuC is inhibited. The authors next show that Mto1 and Mto2 form a {gamma}-TuC-independent complex, and that each protein binds only weakly to {gamma}-TuC in the absence of the other. They conclude that Mto1 and Mto2 act cooperatively to promote the association of the Mto1/2 complex with {gamma}-TuC.


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Related articles in JCS:

Two distinct regions of Mto1 are required for normal microtubule nucleation and efficient association with the {gamma}-tubulin complex in vivo
Itaru Samejima, Victoria J. Miller, Lynda M. Groocock, and Kenneth E. Sawin
JCS 2008 121: 3971-3980. [Abstract] [Full Text]  




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