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Aurora A contributes to p150ᵍⁱᵘᵉᵈ phosphorylation and function during mitosis

Romé, Pierre and Montembault, Emilie and Franck, Nathalie and Pascal, Aude and Glover, David M. and Giet, Régis (2010) Aurora A contributes to p150ᵍⁱᵘᵉᵈ phosphorylation and function during mitosis. Journal of Cell Biology, 189 (4). pp. 651-659. ISSN 1540-8140. PMCID PMC2872913. https://resolver.caltech.edu/CaltechAUTHORS:20200807-170352522

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[img] Video (QuickTime) (Video 1. Dynamics of p150-GFP protein in a Drosophila S2 cell) - Supplemental Material
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[img] Video (QuickTime) (Video 2. Dynamics of p150-SA8-GFP protein in a Drosophila S2 cell) - Supplemental Material
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[img] MS PowerPoint (Figure 1. p150glued is an aurora A substrate in vitro) - Supplemental Material
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[img] MS PowerPoint (Figure 2. The MBD of p150glued is phosphorylated by aurora A after nuclear envelope breakdown) - Supplemental Material
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[img] MS PowerPoint (Figure 3. A full-length p150glued that can no longer be phosphorylated by aurora A binds more strongly to microtubules but cannot rescue glued spindle assembly defect.) - Supplemental Material
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[img] MS PowerPoint (Figure 4. p150-SA8-GFP displays higher affinity for microtubules than wild-type p150-GFP protein during mitosis) - Supplemental Material
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[img] MS PowerPoint (Figure 5. p150glued accumulates at spindle poles of aurora A RNAi-deficient S2 cells and aurora A mutant neuroblasts) - Supplemental Material
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Abstract

Aurora A is a spindle pole–associated protein kinase required for mitotic spindle assembly and chromosome segregation. In this study, we show that Drosophila melanogaster aurora A phosphorylates the dynactin subunit p150ᵍⁱᵘᵉᵈ on sites required for its association with the mitotic spindle. Dynactin strongly accumulates on microtubules during prophase but disappears as soon as the nuclear envelope breaks down, suggesting that its spindle localization is tightly regulated. If aurora A's function is compromised, dynactin and dynein become enriched on mitotic spindle microtubules. Phosphorylation sites are localized within the conserved microtubule-binding domain (MBD) of the p150ᵍⁱᵘᵉᵈ. Although wild-type p150ᵍⁱᵘᵉᵈ binds weakly to spindle microtubules, a variant that can no longer be phosphorylated by aurora A remains associated with spindle microtubules and fails to rescue depletion of endogenous p150ᵍⁱᵘᵉᵈ. Our results suggest that aurora A kinase participates in vivo to the phosphoregulation of the p150ᵍⁱᵘᵉᵈ MBD to limit the microtubule binding of the dynein–dynactin complex and thus regulates spindle assembly.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1083/jcb.201001144DOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872913/PubMed CentralArticle
ORCID:
AuthorORCID
Romé, Pierre0000-0001-5611-5323
Montembault, Emilie0000-0002-4850-3622
Glover, David M.0000-0003-0956-0103
Giet, Régis0000-0001-9027-5849
Alternate Title:Aurora A contributes to p150glued phosphorylation and function during mitosis
Additional Information:© 2010 Romé et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). Submitted: 26 January 2010. Accepted: 19 April 2010. We thank the laboratory members for stimulating discussions, Clotilde Petretti, Thomas Hays, Pier Paolo d'Avino, Gilles Hickson, and Arnaud Echard for reagents, and Stéphanie Dutertre for microscopy facilities of the IFR140. R. Giet thanks Kathryn Lilley for initial proteomic studies and the members of David Glover's group in Cambridge, where this project was initiated (Department of Genetics, University of Cambridge, Cambridge, England, UK). Special thanks are due to Claude Prigent for his full support and to Alex Holmes, Emeric Sevin, and M. Savoian for their critical reading of the manuscript. R. Giet and N. Franck are funded by the Agence Nationale de la Recherche (programme Jeune Chercheur) and the Ligue Nationale Contre le Cancer (Equipe Labellisée). E. Montembault and P. Romé are doctoral fellows of the French Ministère de la Recherche.
Funders:
Funding AgencyGrant Number
Agence Nationale pour la Recherche (ANR)Jeune Chercheur
Ligue Nationale Contre le CancerUNSPECIFIED
Ministère de la RechercheUNSPECIFIED
Issue or Number:4
PubMed Central ID:PMC2872913
Record Number:CaltechAUTHORS:20200807-170352522
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20200807-170352522
Official Citation:Pierre Romé, Emilie Montembault, Nathalie Franck, Aude Pascal, David M. Glover, Régis Giet; Aurora A contributes to p150glued phosphorylation and function during mitosis. J Cell Biol 17 May 2010; 189 (4): 651–659. doi: https://doi.org/10.1083/jcb.201001144
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:104857
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:19 Aug 2020 21:59
Last Modified:19 Aug 2020 21:59

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