Augmin : a protein complex required for centrosome-independent microtubule generation within the spindle


a service of the MBLWHOI Library | About WHOAS

Show simple item record

dc.contributor.author Goshima, Gohta
dc.contributor.author Mayer, Mirjam
dc.contributor.author Zhang, Nan
dc.contributor.author Stuurman, Nico
dc.contributor.author Vale, Ronald D.
dc.date.accessioned 2008-12-30T19:43:21Z
dc.date.available 2008-12-30T19:43:21Z
dc.date.issued 2008-04-28
dc.identifier.citation Journal of Cell Biology 181 (2008): 421-429 en
dc.identifier.uri http://hdl.handle.net/1912/2621
dc.description © 2008 Goshima et al. This article is distributed under the terms of a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license). The definitive version was published in Journal of Cell Biology 181 (2008): 421-429, doi:10.1083/jcb.200711053. en
dc.description.abstract Since the discovery of γ-tubulin, attention has focused on its involvement as a microtubule nucleator at the centrosome. However, mislocalization of {gamma}-tubulin away from the centrosome does not inhibit mitotic spindle formation in Drosophila melanogaster, suggesting that a critical function for γ-tubulin might reside elsewhere. A previous RNA interference (RNAi) screen identified five genes (Dgt2–6) required for localizing γ-tubulin to spindle microtubules. We show that the Dgt proteins interact, forming a stable complex. We find that spindle microtubule generation is substantially reduced after knockdown of each Dgt protein by RNAi. Thus, the Dgt complex that we name "augmin" functions to increase microtubule number. Reduced spindle microtubule generation after augmin RNAi, particularly in the absence of functional centrosomes, has dramatic consequences on mitotic spindle formation and function, leading to reduced kinetochore fiber formation, chromosome misalignment, and spindle bipolarity defects. We also identify a functional human homologue of Dgt6. Our results suggest that an important mitotic function for γ-tubulin may lie within the spindle, where augmin and γ-tubulin function cooperatively to amplify the number of microtubules. en
dc.description.sponsorship This work is supported by the Special Coordination Funds for Promoting Science and Technology (MEXT, Japan), the Global COE Program “Advanced Systems-Biology: Designing the Biological Function” (MEXT), and the Uehara Memorial Foundation. en
dc.format.mimetype video/quicktime
dc.format.mimetype application/pdf
dc.format.mimetype image/jpeg
dc.language.iso en_US en
dc.publisher Rockefeller University Press en
dc.relation.uri http://dx.doi.org/10.1083/jcb.200711053
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/ *
dc.title Augmin : a protein complex required for centrosome-independent microtubule generation within the spindle en
dc.type Article en
dc.identifier.doi 10.1083/jcb.200711053

Files in this item

The following license files are associated with this item:

This item appears in the following Collection(s)

Show simple item record

http://creativecommons.org/licenses/by-nc-sa/3.0/ Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/3.0/

Search WHOAS


My Account