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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...

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Detalles Bibliográficos
Autores principales: Soppina, Virupakshi, Verhey, Kristen J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2014
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.
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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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