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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2019
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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. |
format | Online Article Text |
id | pubmed-6899999 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT belshamhannahr identificationofkeyresiduesthatregulatetheinteractionofkinesinswithmicrotubuleends AT frielclairet identificationofkeyresiduesthatregulatetheinteractionofkinesinswithmicrotubuleends |