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Identification of key residues that regulate the interaction of kinesins with microtubule ends

Kinesins are molecular motors that use energy derived from ATP turnover to walk along microtubules, or when at the microtubule end, regulate growth or shrinkage. All kinesins that regulate microtubule dynamics have long residence times at microtubule ends, whereas those that only walk have short end...

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Detalles Bibliográficos
Autores principales: Belsham, Hannah R., Friel, Claire T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899999/
https://www.ncbi.nlm.nih.gov/pubmed/31574569
http://dx.doi.org/10.1002/cm.21568
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author Belsham, Hannah R.
Friel, Claire T.
author_facet Belsham, Hannah R.
Friel, Claire T.
author_sort Belsham, Hannah R.
collection PubMed
description Kinesins are molecular motors that use energy derived from ATP turnover to walk along microtubules, or when at the microtubule end, regulate growth or shrinkage. All kinesins that regulate microtubule dynamics have long residence times at microtubule ends, whereas those that only walk have short end‐residence times. Here, we identify key amino acids involved in end binding by showing that when critical residues from Kinesin‐13, which depolymerises microtubules, are introduced into Kinesin‐1, a walking kinesin with no effect on microtubule dynamics, the end‐residence time is increased up to several‐fold. This indicates that the interface between the kinesin motor domain and the microtubule is malleable and can be tuned to favour either lattice or end binding.
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spelling pubmed-68999992019-12-20 Identification of key residues that regulate the interaction of kinesins with microtubule ends Belsham, Hannah R. Friel, Claire T. Cytoskeleton (Hoboken) Research Articles Kinesins are molecular motors that use energy derived from ATP turnover to walk along microtubules, or when at the microtubule end, regulate growth or shrinkage. All kinesins that regulate microtubule dynamics have long residence times at microtubule ends, whereas those that only walk have short end‐residence times. Here, we identify key amino acids involved in end binding by showing that when critical residues from Kinesin‐13, which depolymerises microtubules, are introduced into Kinesin‐1, a walking kinesin with no effect on microtubule dynamics, the end‐residence time is increased up to several‐fold. This indicates that the interface between the kinesin motor domain and the microtubule is malleable and can be tuned to favour either lattice or end binding. John Wiley & Sons, Inc. 2019-10-21 2019 /pmc/articles/PMC6899999/ /pubmed/31574569 http://dx.doi.org/10.1002/cm.21568 Text en © 2019 The Authors. Cytoskeleton published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Belsham, Hannah R.
Friel, Claire T.
Identification of key residues that regulate the interaction of kinesins with microtubule ends
title Identification of key residues that regulate the interaction of kinesins with microtubule ends
title_full Identification of key residues that regulate the interaction of kinesins with microtubule ends
title_fullStr Identification of key residues that regulate the interaction of kinesins with microtubule ends
title_full_unstemmed Identification of key residues that regulate the interaction of kinesins with microtubule ends
title_short Identification of key residues that regulate the interaction of kinesins with microtubule ends
title_sort identification of key residues that regulate the interaction of kinesins with microtubule ends
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899999/
https://www.ncbi.nlm.nih.gov/pubmed/31574569
http://dx.doi.org/10.1002/cm.21568
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