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Why motor proteins team up - Intraflagellar transport in C. elegans cilia

Inside the cell, vital processes such as cell division and intracellular transport are driven by the concerted action of different molecular motor proteins. In C. elegans chemosensory cilia, 2 kinesin-2 family motor proteins, kinesin-II and OSM-3, team up to drive intraflagellar transport (IFT) in t...

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Detalles Bibliográficos
Autores principales: Mijalkovic, Jona, Prevo, Bram, Peterman, Erwin J. G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4911997/
https://www.ncbi.nlm.nih.gov/pubmed/27384150
http://dx.doi.org/10.1080/21624054.2016.1170275
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author Mijalkovic, Jona
Prevo, Bram
Peterman, Erwin J. G.
author_facet Mijalkovic, Jona
Prevo, Bram
Peterman, Erwin J. G.
author_sort Mijalkovic, Jona
collection PubMed
description Inside the cell, vital processes such as cell division and intracellular transport are driven by the concerted action of different molecular motor proteins. In C. elegans chemosensory cilia, 2 kinesin-2 family motor proteins, kinesin-II and OSM-3, team up to drive intraflagellar transport (IFT) in the anterograde direction, from base to tip, whereas IFT dynein hitchhikes toward the tip and subsequently drives IFT in the opposite, retrograde direction, thereby recycling both kinesins. While it is evident that at least a retrograde and an anterograde motor are necessary to drive IFT, it has remained puzzling why 2 same-polarity kinesins are employed. Recently, we addressed this question by combining advanced genome-engineering tools with ultrasensitive, quantitative fluorescence microscopy to study IFT with single-molecule sensitivity.(1,2) Using this combination of approaches, we uncovered a differentiation in kinesin-2 function, in which the slower kinesin-II operates as an ‘importer’, loading IFT trains into the cilium before gradually handing them over to the faster OSM-3. OSM-3 subsequently acts as a long-range ‘transporter’, driving the IFT trains toward the tip. The two kinesin-2 motors combine their unique motility properties to achieve something neither motor can achieve on its own; that is to optimize the amount of cargo inside the cilium. In this commentary, we provide detailed insight into the rationale behind our research approach and comment on our recent findings. Moreover, we discuss the role of IFT dynein and provide an outlook on future studies.
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spelling pubmed-49119972016-07-06 Why motor proteins team up - Intraflagellar transport in C. elegans cilia Mijalkovic, Jona Prevo, Bram Peterman, Erwin J. G. Worm Commentary Inside the cell, vital processes such as cell division and intracellular transport are driven by the concerted action of different molecular motor proteins. In C. elegans chemosensory cilia, 2 kinesin-2 family motor proteins, kinesin-II and OSM-3, team up to drive intraflagellar transport (IFT) in the anterograde direction, from base to tip, whereas IFT dynein hitchhikes toward the tip and subsequently drives IFT in the opposite, retrograde direction, thereby recycling both kinesins. While it is evident that at least a retrograde and an anterograde motor are necessary to drive IFT, it has remained puzzling why 2 same-polarity kinesins are employed. Recently, we addressed this question by combining advanced genome-engineering tools with ultrasensitive, quantitative fluorescence microscopy to study IFT with single-molecule sensitivity.(1,2) Using this combination of approaches, we uncovered a differentiation in kinesin-2 function, in which the slower kinesin-II operates as an ‘importer’, loading IFT trains into the cilium before gradually handing them over to the faster OSM-3. OSM-3 subsequently acts as a long-range ‘transporter’, driving the IFT trains toward the tip. The two kinesin-2 motors combine their unique motility properties to achieve something neither motor can achieve on its own; that is to optimize the amount of cargo inside the cilium. In this commentary, we provide detailed insight into the rationale behind our research approach and comment on our recent findings. Moreover, we discuss the role of IFT dynein and provide an outlook on future studies. Taylor & Francis 2016-03-30 /pmc/articles/PMC4911997/ /pubmed/27384150 http://dx.doi.org/10.1080/21624054.2016.1170275 Text en © 2016 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Commentary
Mijalkovic, Jona
Prevo, Bram
Peterman, Erwin J. G.
Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title_full Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title_fullStr Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title_full_unstemmed Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title_short Why motor proteins team up - Intraflagellar transport in C. elegans cilia
title_sort why motor proteins team up - intraflagellar transport in c. elegans cilia
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4911997/
https://www.ncbi.nlm.nih.gov/pubmed/27384150
http://dx.doi.org/10.1080/21624054.2016.1170275
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