Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.

The formation and maintenance of microtubules requires their polymerisation, but little is known about how this polymerisation is regulated in cells. Focussing on the essential microtubule bundles in axons of Drosophila and Xenopus neurons, we show that the plus-end scaffold Eb1, the polymerase XMAP...

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Autores principales:	Ines Hahn, Andre Voelzmann, Jill Parkin, Judith B Fülle, Paula G Slater, Laura Anne Lowery, Natalia Sanchez-Soriano, Andreas Prokop
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Genetics QH426-470
Acceso en línea:	https://doaj.org/article/c5e8e8f422334f6baa0209cb9072db39
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spelling	oai:doaj.org-article:c5e8e8f422334f6baa0209cb9072db392021-12-02T20:02:57ZTau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.1553-73901553-740410.1371/journal.pgen.1009647https://doaj.org/article/c5e8e8f422334f6baa0209cb9072db392021-07-01T00:00:00Zhttps://doi.org/10.1371/journal.pgen.1009647https://doaj.org/toc/1553-7390https://doaj.org/toc/1553-7404The formation and maintenance of microtubules requires their polymerisation, but little is known about how this polymerisation is regulated in cells. Focussing on the essential microtubule bundles in axons of Drosophila and Xenopus neurons, we show that the plus-end scaffold Eb1, the polymerase XMAP215/Msps and the lattice-binder Tau co-operate interdependently to promote microtubule polymerisation and bundle organisation during axon development and maintenance. Eb1 and XMAP215/Msps promote each other's localisation at polymerising microtubule plus-ends. Tau outcompetes Eb1-binding along microtubule lattices, thus preventing depletion of Eb1 tip pools. The three factors genetically interact and show shared mutant phenotypes: reductions in axon growth, comet sizes, comet numbers and comet velocities, as well as prominent deterioration of parallel microtubule bundles into disorganised curled conformations. This microtubule curling is caused by Eb1 plus-end depletion which impairs spectraplakin-mediated guidance of extending microtubules into parallel bundles. Our demonstration that Eb1, XMAP215/Msps and Tau co-operate during the regulation of microtubule polymerisation and bundle organisation, offers new conceptual explanations for developmental and degenerative axon pathologies.Ines HahnAndre VoelzmannJill ParkinJudith B FüllePaula G SlaterLaura Anne LoweryNatalia Sanchez-SorianoAndreas ProkopPublic Library of Science (PLoS)articleGeneticsQH426-470ENPLoS Genetics, Vol 17, Iss 7, p e1009647 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Genetics QH426-470
spellingShingle	Genetics QH426-470 Ines Hahn Andre Voelzmann Jill Parkin Judith B Fülle Paula G Slater Laura Anne Lowery Natalia Sanchez-Soriano Andreas Prokop Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
description	The formation and maintenance of microtubules requires their polymerisation, but little is known about how this polymerisation is regulated in cells. Focussing on the essential microtubule bundles in axons of Drosophila and Xenopus neurons, we show that the plus-end scaffold Eb1, the polymerase XMAP215/Msps and the lattice-binder Tau co-operate interdependently to promote microtubule polymerisation and bundle organisation during axon development and maintenance. Eb1 and XMAP215/Msps promote each other's localisation at polymerising microtubule plus-ends. Tau outcompetes Eb1-binding along microtubule lattices, thus preventing depletion of Eb1 tip pools. The three factors genetically interact and show shared mutant phenotypes: reductions in axon growth, comet sizes, comet numbers and comet velocities, as well as prominent deterioration of parallel microtubule bundles into disorganised curled conformations. This microtubule curling is caused by Eb1 plus-end depletion which impairs spectraplakin-mediated guidance of extending microtubules into parallel bundles. Our demonstration that Eb1, XMAP215/Msps and Tau co-operate during the regulation of microtubule polymerisation and bundle organisation, offers new conceptual explanations for developmental and degenerative axon pathologies.
format	article
author	Ines Hahn Andre Voelzmann Jill Parkin Judith B Fülle Paula G Slater Laura Anne Lowery Natalia Sanchez-Soriano Andreas Prokop
author_facet	Ines Hahn Andre Voelzmann Jill Parkin Judith B Fülle Paula G Slater Laura Anne Lowery Natalia Sanchez-Soriano Andreas Prokop
author_sort	Ines Hahn
title	Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
title_short	Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
title_full	Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
title_fullStr	Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
title_full_unstemmed	Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
title_sort	tau, xmap215/msps and eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/c5e8e8f422334f6baa0209cb9072db39
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Tau, XMAP215/Msps and Eb1 co-operate interdependently to regulate microtubule polymerisation and bundle formation in axons.

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