MozartV1, France, Analysis, bibRecord, 000008

γ-Tubulin Ring Complexes and EB1 play antagonistic roles in microtubule dynamics and spindle positioning

Identifieur interne : 000008 ( France/Analysis ); précédent : 000007; suivant : 000009

γ-Tubulin Ring Complexes and EB1 play antagonistic roles in microtubule dynamics and spindle positioning

Auteurs : Ana S Bouissou [France] ; Christel Vérollet [France] ; Hélène De Forges [France] ; Laurence Haren [France] ; Yohanns Bella Che [France] ; Franck Perez [France] ; Andreas Merdes [France] ; Brigitte Raynaud-Messina [France]

Source :

The EMBO Journal [ 0261-4189 ] ; 2014.

RBID : PMC:3989606

Abstract

γ-Tubulin is critical for microtubule (MT) assembly and organization. In metazoa, this protein acts in multiprotein complexes called γ-Tubulin Ring Complexes (γ-TuRCs). While the subunits that constitute γ-Tubulin Small Complexes (γ-TuSCs), the core of the MT nucleation machinery, are essential, mutation of γ-TuRC-specific proteins in Drosophila causes sterility and morphological abnormalities via hitherto unidentified mechanisms. Here, we demonstrate a role of γ-TuRCs in controlling spindle orientation independent of MT nucleation activity, both in cultured cells and in vivo, and examine a potential function for γ-TuRCs on astral MTs. γ-TuRCs locate along the length of astral MTs, and depletion of γ-TuRC-specific proteins increases MT dynamics and causes the plus-end tracking protein EB1 to redistribute along MTs. Moreover, suppression of MT dynamics through drug treatment or EB1 down-regulation rescues spindle orientation defects induced by γ-TuRC depletion. Therefore, we propose a role for γ-TuRCs in regulating spindle positioning by controlling the stability of astral MTs.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3989606

DOI: 10.1002/embj.201385967
PubMed: 24421324
PubMed Central: 3989606

Affiliations:

France

Links to Exploration step

PMC:3989606

Le document en format XML

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<author><name sortKey="Bouissou, Ana S" sort="Bouissou, Ana S" uniqKey="Bouissou A" first="Ana S" last="Bouissou">Ana S Bouissou</name>
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<front><div type="abstract" xml:lang="en"><p>γ-Tubulin is critical for microtubule (MT) assembly and organization. In metazoa, this protein acts in multiprotein complexes called γ-Tubulin Ring Complexes (γ-TuRCs). While the subunits that constitute γ-Tubulin Small Complexes (γ-TuSCs), the core of the MT nucleation machinery, are essential, mutation of γ-TuRC-specific proteins in <italic>Drosophila</italic>
 causes sterility and morphological abnormalities via hitherto unidentified mechanisms. Here, we demonstrate a role of γ-TuRCs in controlling spindle orientation independent of MT nucleation activity, both in cultured cells and <italic>in vivo</italic>
, and examine a potential function for γ-TuRCs on astral MTs. γ-TuRCs locate along the length of astral MTs, and depletion of γ-TuRC-specific proteins increases MT dynamics and causes the plus-end tracking protein EB1 to redistribute along MTs. Moreover, suppression of MT dynamics through drug treatment or EB1 down-regulation rescues spindle orientation defects induced by γ-TuRC depletion. Therefore, we propose a role for γ-TuRCs in regulating spindle positioning by controlling the stability of astral MTs.</p>
</div>
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<name sortKey="Bella Che, Yohanns" sort="Bella Che, Yohanns" uniqKey="Bella Che Y" first="Yohanns" last="Bella Che">Yohanns Bella Che</name>
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γ-Tubulin Ring Complexes and EB1 play antagonistic roles in microtubule dynamics and spindle positioning

γ-Tubulin Ring Complexes and EB1 play antagonistic roles in microtubule dynamics and spindle positioning

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Abstract

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