The nucleoporin MEL-28 promotes RanGTP-dependent γ-tubulin recruitment and microtubule nucleation in mitotic spindle formation
Hideki Yokoyama (),
Birgit Koch,
Rudolf Walczak,
Fulya Ciray-Duygu,
Juan Carlos González-Sánchez,
Damien P. Devos,
Iain W. Mattaj and
Oliver J. Gruss
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Hideki Yokoyama: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Birgit Koch: European Molecular Biology Laboratory
Rudolf Walczak: European Molecular Biology Laboratory
Fulya Ciray-Duygu: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Juan Carlos González-Sánchez: Centre for Organismal Studies (COS)
Damien P. Devos: Centre for Organismal Studies (COS)
Iain W. Mattaj: European Molecular Biology Laboratory
Oliver J. Gruss: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance
Nature Communications, 2014, vol. 5, issue 1, 1-9
Abstract:
Abstract The GTP-bound form of the Ran GTPase (RanGTP), produced around chromosomes, drives nuclear envelope and nuclear pore complex (NPC) re-assembly after mitosis. The nucleoporin MEL-28/ELYS binds chromatin in a RanGTP-regulated manner and acts to seed NPC assembly. Here we show that, upon mitotic NPC disassembly, MEL-28 dissociates from chromatin and re-localizes to spindle microtubules and kinetochores. MEL-28 directly binds microtubules in a RanGTP-regulated way via its C-terminal chromatin-binding domain. Using Xenopus egg extracts, we demonstrate that MEL-28 is essential for RanGTP-dependent microtubule nucleation and spindle assembly, independent of its function in NPC assembly. Specifically, MEL-28 interacts with the γ-tubulin ring complex and recruits it to microtubule nucleation sites. Our data identify MEL-28 as a RanGTP target that functions throughout the cell cycle. Its cell cycle-dependent binding to chromatin or microtubules discriminates MEL-28 functions in interphase and mitosis, and ensures that spindle assembly occurs only after NPC breakdown.
Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4270
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DOI: 10.1038/ncomms4270
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