First published online November 19, 2008
Journal of Cell Science 121, 2305e (2008)
© The Company of Biologists Limited
Mto1/2 gets microtubules going
During nucleation – an essential early step in de novo formation of microtubules – the
-tubulin complex (
-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
-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
-TuC. The authors first show that, similar to
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
-TuC, although it localises normally and interacts with Mto2. By contrast, mutations outside the CM1 region of Mto1 phenocopy
mto2 yeast – limited microtubule nucleation does occur, but binding of Mto1 to Mto2 or
-TuC is inhibited. The authors next show that Mto1 and Mto2 form a
-TuC-independent complex, and that each protein binds only weakly to
-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
-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
-tubulin complex in vivo
- Itaru Samejima, Victoria J. Miller, Lynda M. Groocock, and Kenneth E. Sawin
JCS 2008 121: 3971-3980.
[Abstract]
[Full Text]