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The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors
The kinesin-3 family (KIF) is one of the largest among the kinesin superfamily and an important driver of a variety of cellular transport events. Whereas all kinesins contain the highly conserved kinesin motor domain, different families have evolved unique motor features that enable different mechan...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091829/ https://www.ncbi.nlm.nih.gov/pubmed/24850887 http://dx.doi.org/10.1091/mbc.E14-01-0696 |
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author | Soppina, Virupakshi Verhey, Kristen J. |
author_facet | Soppina, Virupakshi Verhey, Kristen J. |
author_sort | Soppina, Virupakshi |
collection | PubMed |
description | The kinesin-3 family (KIF) is one of the largest among the kinesin superfamily and an important driver of a variety of cellular transport events. Whereas all kinesins contain the highly conserved kinesin motor domain, different families have evolved unique motor features that enable different mechanical and functional outputs. A defining feature of kinesin-3 motors is the presence of a positively charged insert, the K-loop, in loop 12 of their motor domains. However, the mechanical and functional output of the K-loop with respect to processive motility of dimeric kinesin-3 motors is unknown. We find that, surprisingly, the K-loop plays no role in generating the superprocessive motion of dimeric kinesin-3 motors (KIF1, KIF13, and KIF16). Instead, we find that the K-loop provides kinesin-3 motors with a high microtubule affinity in the motor's ADP-bound state, a state that for other kinesins binds only weakly to the microtubule surface. A high microtubule affinity results in a high landing rate of processive kinesin-3 motors on the microtubule surface. We propose that the family-specific K-loop contributes to efficient kinesin-3 cargo transport by enhancing the initial interaction of dimeric motors with the microtubule track. |
format | Online Article Text |
id | pubmed-4091829 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-40918292014-10-01 The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors Soppina, Virupakshi Verhey, Kristen J. Mol Biol Cell Articles The kinesin-3 family (KIF) is one of the largest among the kinesin superfamily and an important driver of a variety of cellular transport events. Whereas all kinesins contain the highly conserved kinesin motor domain, different families have evolved unique motor features that enable different mechanical and functional outputs. A defining feature of kinesin-3 motors is the presence of a positively charged insert, the K-loop, in loop 12 of their motor domains. However, the mechanical and functional output of the K-loop with respect to processive motility of dimeric kinesin-3 motors is unknown. We find that, surprisingly, the K-loop plays no role in generating the superprocessive motion of dimeric kinesin-3 motors (KIF1, KIF13, and KIF16). Instead, we find that the K-loop provides kinesin-3 motors with a high microtubule affinity in the motor's ADP-bound state, a state that for other kinesins binds only weakly to the microtubule surface. A high microtubule affinity results in a high landing rate of processive kinesin-3 motors on the microtubule surface. We propose that the family-specific K-loop contributes to efficient kinesin-3 cargo transport by enhancing the initial interaction of dimeric motors with the microtubule track. The American Society for Cell Biology 2014-07-15 /pmc/articles/PMC4091829/ /pubmed/24850887 http://dx.doi.org/10.1091/mbc.E14-01-0696 Text en © 2014 Soppina and Verhey. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Soppina, Virupakshi Verhey, Kristen J. The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title | The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title_full | The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title_fullStr | The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title_full_unstemmed | The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title_short | The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
title_sort | family-specific k-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091829/ https://www.ncbi.nlm.nih.gov/pubmed/24850887 http://dx.doi.org/10.1091/mbc.E14-01-0696 |
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