Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro

Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubule...

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Detalles Bibliográficos
Autores principales: Walter, Wilhelm J., Beránek, Václav, Fischermeier, Elisabeth, Diez, Stefan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3411631/
https://www.ncbi.nlm.nih.gov/pubmed/22870307
http://dx.doi.org/10.1371/journal.pone.0042218
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author Walter, Wilhelm J.
Beránek, Václav
Fischermeier, Elisabeth
Diez, Stefan
author_facet Walter, Wilhelm J.
Beránek, Václav
Fischermeier, Elisabeth
Diez, Stefan
author_sort Walter, Wilhelm J.
collection PubMed
description Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length.
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spelling pubmed-34116312012-08-06 Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro Walter, Wilhelm J. Beránek, Václav Fischermeier, Elisabeth Diez, Stefan PLoS One Research Article Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length. Public Library of Science 2012-08-01 /pmc/articles/PMC3411631/ /pubmed/22870307 http://dx.doi.org/10.1371/journal.pone.0042218 Text en © 2012 Walter et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Walter, Wilhelm J.
Beránek, Václav
Fischermeier, Elisabeth
Diez, Stefan
Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title_full Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title_fullStr Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title_full_unstemmed Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title_short Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
title_sort tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3411631/
https://www.ncbi.nlm.nih.gov/pubmed/22870307
http://dx.doi.org/10.1371/journal.pone.0042218
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AT fischermeierelisabeth tubulinacetylationalonedoesnotaffectkinesin1velocityandrunlengthinvitro
AT diezstefan tubulinacetylationalonedoesnotaffectkinesin1velocityandrunlengthinvitro

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