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Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms
Long-distance transport in cells is driven by kinesin and dynein motors that move along microtubule tracks. These motors must be tightly regulated to ensure the spatial and temporal fidelity of their transport events. Transport motors of the kinesin-1 and kinesin-3 families are regulated by autoinhi...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886353/ https://www.ncbi.nlm.nih.gov/pubmed/20530208 http://dx.doi.org/10.1083/jcb.201001057 |
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author | Hammond, Jennetta W. Blasius, T. Lynne Soppina, Virupakshi Cai, Dawen Verhey, Kristen J. |
author_facet | Hammond, Jennetta W. Blasius, T. Lynne Soppina, Virupakshi Cai, Dawen Verhey, Kristen J. |
author_sort | Hammond, Jennetta W. |
collection | PubMed |
description | Long-distance transport in cells is driven by kinesin and dynein motors that move along microtubule tracks. These motors must be tightly regulated to ensure the spatial and temporal fidelity of their transport events. Transport motors of the kinesin-1 and kinesin-3 families are regulated by autoinhibition, but little is known about the mechanisms that regulate kinesin-2 motors. We show that the homodimeric kinesin-2 motor KIF17 is kept in an inactive state in the absence of cargo. Autoinhibition is caused by a folded conformation that enables nonmotor regions to directly contact and inhibit the enzymatic activity of the motor domain. We define two molecular mechanisms that contribute to autoinhibition of KIF17. First, the C-terminal tail interferes with microtubule binding; and second, a coiled-coil segment blocks processive motility. The latter is a new mechanism for regulation of kinesin motors. This work supports the model that autoinhibition is a general mechanism for regulation of kinesin motors involved in intracellular trafficking events. |
format | Text |
id | pubmed-2886353 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28863532010-12-14 Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms Hammond, Jennetta W. Blasius, T. Lynne Soppina, Virupakshi Cai, Dawen Verhey, Kristen J. J Cell Biol Research Articles Long-distance transport in cells is driven by kinesin and dynein motors that move along microtubule tracks. These motors must be tightly regulated to ensure the spatial and temporal fidelity of their transport events. Transport motors of the kinesin-1 and kinesin-3 families are regulated by autoinhibition, but little is known about the mechanisms that regulate kinesin-2 motors. We show that the homodimeric kinesin-2 motor KIF17 is kept in an inactive state in the absence of cargo. Autoinhibition is caused by a folded conformation that enables nonmotor regions to directly contact and inhibit the enzymatic activity of the motor domain. We define two molecular mechanisms that contribute to autoinhibition of KIF17. First, the C-terminal tail interferes with microtubule binding; and second, a coiled-coil segment blocks processive motility. The latter is a new mechanism for regulation of kinesin motors. This work supports the model that autoinhibition is a general mechanism for regulation of kinesin motors involved in intracellular trafficking events. The Rockefeller University Press 2010-06-14 /pmc/articles/PMC2886353/ /pubmed/20530208 http://dx.doi.org/10.1083/jcb.201001057 Text en © 2010 Hammond et al. https://creativecommons.org/licenses/by-nc-sa/3.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ (https://creativecommons.org/licenses/by-nc-sa/3.0/) ). |
spellingShingle | Research Articles Hammond, Jennetta W. Blasius, T. Lynne Soppina, Virupakshi Cai, Dawen Verhey, Kristen J. Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title | Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title_full | Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title_fullStr | Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title_full_unstemmed | Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title_short | Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms |
title_sort | autoinhibition of the kinesin-2 motor kif17 via dual intramolecular mechanisms |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886353/ https://www.ncbi.nlm.nih.gov/pubmed/20530208 http://dx.doi.org/10.1083/jcb.201001057 |
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