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Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules
Kinesin molecules are motor proteins capable of moving along microtubule by hydrolyzing ATP. They generally have several forms of construct. This review focuses on two of the most studied forms: monomers such as KIF1A (kinesin-3 family) and dimers such as conventional kinesin (kinesin-1 family), bot...
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Formato: | Texto |
Lenguaje: | English |
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Ivyspring International Publisher
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2974169/ https://www.ncbi.nlm.nih.gov/pubmed/21060728 |
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author | Xie, Ping |
author_facet | Xie, Ping |
author_sort | Xie, Ping |
collection | PubMed |
description | Kinesin molecules are motor proteins capable of moving along microtubule by hydrolyzing ATP. They generally have several forms of construct. This review focuses on two of the most studied forms: monomers such as KIF1A (kinesin-3 family) and dimers such as conventional kinesin (kinesin-1 family), both of which can move processively towards the microtubule plus end. There now exist numerous models that try to explain how the kinesin molecules convert the chemical energy of ATP hydrolysis into the mechanical energy to “power” their proceesive movement along microtubule. Here, we attempt to present a comprehensive review of these models. We further propose a new hybrid model for the dimeric kinesin by combining the existing models and provide a framework for future studies in this subject. |
format | Text |
id | pubmed-2974169 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-29741692010-11-08 Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules Xie, Ping Int J Biol Sci Review Kinesin molecules are motor proteins capable of moving along microtubule by hydrolyzing ATP. They generally have several forms of construct. This review focuses on two of the most studied forms: monomers such as KIF1A (kinesin-3 family) and dimers such as conventional kinesin (kinesin-1 family), both of which can move processively towards the microtubule plus end. There now exist numerous models that try to explain how the kinesin molecules convert the chemical energy of ATP hydrolysis into the mechanical energy to “power” their proceesive movement along microtubule. Here, we attempt to present a comprehensive review of these models. We further propose a new hybrid model for the dimeric kinesin by combining the existing models and provide a framework for future studies in this subject. Ivyspring International Publisher 2010-11-03 /pmc/articles/PMC2974169/ /pubmed/21060728 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. |
spellingShingle | Review Xie, Ping Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title | Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title_full | Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title_fullStr | Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title_full_unstemmed | Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title_short | Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules |
title_sort | mechanism of processive movement of monomeric and dimeric kinesin molecules |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2974169/ https://www.ncbi.nlm.nih.gov/pubmed/21060728 |
work_keys_str_mv | AT xieping mechanismofprocessivemovementofmonomericanddimerickinesinmolecules |