On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN

Alignment of the mitotic spindle to the cellular polarity axis is a prerequisite for asymmetric cell divisions. The protein network coordinating the spindle position with cortical polarity includes the molecular machinery pulling on astral microtubules, which is assembled on conserved NuMA:LGN:Gαi c...

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Detalles Bibliográficos
Autores principales: Mapelli, Marina, Gonzalez, Cayetano
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2012
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438535/
https://www.ncbi.nlm.nih.gov/pubmed/22977735
http://dx.doi.org/10.1098/rsob.120102
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author Mapelli, Marina
Gonzalez, Cayetano
author_facet Mapelli, Marina
Gonzalez, Cayetano
author_sort Mapelli, Marina
collection PubMed
description Alignment of the mitotic spindle to the cellular polarity axis is a prerequisite for asymmetric cell divisions. The protein network coordinating the spindle position with cortical polarity includes the molecular machinery pulling on astral microtubules, which is assembled on conserved NuMA:LGN:Gαi complexes, the polarity proteins Par3:Par6:aPKC and an adaptor molecule known as Inscuteable (Insc). To date, all these components were assumed to enter a macromolecular complex localized at polarity sites in mitosis. However, recent structural studies revealed the Insc and NuMA are mutually exclusive interactors of LGN, implying that the molecular mechanism of spindle coupling to polarity is more sophisticated than has been believed to date.
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spelling pubmed-34385352012-09-13 On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN Mapelli, Marina Gonzalez, Cayetano Open Biol Review Alignment of the mitotic spindle to the cellular polarity axis is a prerequisite for asymmetric cell divisions. The protein network coordinating the spindle position with cortical polarity includes the molecular machinery pulling on astral microtubules, which is assembled on conserved NuMA:LGN:Gαi complexes, the polarity proteins Par3:Par6:aPKC and an adaptor molecule known as Inscuteable (Insc). To date, all these components were assumed to enter a macromolecular complex localized at polarity sites in mitosis. However, recent structural studies revealed the Insc and NuMA are mutually exclusive interactors of LGN, implying that the molecular mechanism of spindle coupling to polarity is more sophisticated than has been believed to date. The Royal Society 2012-08 /pmc/articles/PMC3438535/ /pubmed/22977735 http://dx.doi.org/10.1098/rsob.120102 Text en http://creativecommons.org/licenses/by/3.0/ © 2012 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Review
Mapelli, Marina
Gonzalez, Cayetano
On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title_full On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title_fullStr On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title_full_unstemmed On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title_short On the inscrutable role of Inscuteable: structural basis and functional implications for the competitive binding of NuMA and Inscuteable to LGN
title_sort on the inscrutable role of inscuteable: structural basis and functional implications for the competitive binding of numa and inscuteable to lgn
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438535/
https://www.ncbi.nlm.nih.gov/pubmed/22977735
http://dx.doi.org/10.1098/rsob.120102
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