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Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load

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Title: Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load
Authors: Hendricks, Adam G.1 adhendri@umich.edu, Epureanu, Bogdan I.1 epureanu@umich.edu, Meyhöfer, Edgar2 meyhofer@umich.edu
Source: Physica D. Apr2009, Vol. 238 Issue 6, p677-686. 10p.
Subjects: Kinesin, Adenosine triphosphate, Mechanical behavior of materials, Microtubules, Brownian motion, Unsteady flow, Quantum perturbations, Transients (Dynamics)
Abstract: Abstract: Recent experiments using single-molecule techniques have characterized the mechanical properties of single kinesin molecules in vitro at a range of loads and ATP concentrations. These experiments have shown that kinesin moves processively along microtubules by alternately advancing each of its motor domains in a hand-over-hand fashion, using Brownian motion and the energy from ATP hydrolysis. We have extended the theoretical analysis of kinesin through a mechanistic model that is capable of describing transient and steady-state behavior. Transient dynamics are needed to describe the effect of external perturbations (e.g. interactions with other kinesin molecules). Quantitative metrics are tailored to characterize the synchronization of nonlinear, nonsmooth systems such as kinesin. These metrics are employed to analyze the simulation results and to quantify the effect of the cargo linker stiffness, the load, and the difference in intrinsic velocity on the synchronization of two coupled motor proteins. Herein, the mechanistic model and the new analysis techniques are demonstrated for the case of two coupled kinesin motors. [Copyright &y& Elsevier]
Copyright of Physica D is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 36895970
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load
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  Data: <searchLink fieldCode="AR" term="%22Hendricks%2C+Adam+G%2E%22">Hendricks, Adam G.</searchLink><relatesTo>1</relatesTo><i> adhendri@umich.edu</i><br /><searchLink fieldCode="AR" term="%22Epureanu%2C+Bogdan+I%2E%22">Epureanu, Bogdan I.</searchLink><relatesTo>1</relatesTo><i> epureanu@umich.edu</i><br /><searchLink fieldCode="AR" term="%22Meyhöfer%2C+Edgar%22">Meyhöfer, Edgar</searchLink><relatesTo>2</relatesTo><i> meyhofer@umich.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Physica+D%22">Physica D</searchLink>. Apr2009, Vol. 238 Issue 6, p677-686. 10p.
– Name: Subject
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  Data: <searchLink fieldCode="DE" term="%22Kinesin%22">Kinesin</searchLink><br /><searchLink fieldCode="DE" term="%22Adenosine+triphosphate%22">Adenosine triphosphate</searchLink><br /><searchLink fieldCode="DE" term="%22Mechanical+behavior+of+materials%22">Mechanical behavior of materials</searchLink><br /><searchLink fieldCode="DE" term="%22Microtubules%22">Microtubules</searchLink><br /><searchLink fieldCode="DE" term="%22Brownian+motion%22">Brownian motion</searchLink><br /><searchLink fieldCode="DE" term="%22Unsteady+flow%22">Unsteady flow</searchLink><br /><searchLink fieldCode="DE" term="%22Quantum+perturbations%22">Quantum perturbations</searchLink><br /><searchLink fieldCode="DE" term="%22Transients+%28Dynamics%29%22">Transients (Dynamics)</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Abstract: Recent experiments using single-molecule techniques have characterized the mechanical properties of single kinesin molecules in vitro at a range of loads and ATP concentrations. These experiments have shown that kinesin moves processively along microtubules by alternately advancing each of its motor domains in a hand-over-hand fashion, using Brownian motion and the energy from ATP hydrolysis. We have extended the theoretical analysis of kinesin through a mechanistic model that is capable of describing transient and steady-state behavior. Transient dynamics are needed to describe the effect of external perturbations (e.g. interactions with other kinesin molecules). Quantitative metrics are tailored to characterize the synchronization of nonlinear, nonsmooth systems such as kinesin. These metrics are employed to analyze the simulation results and to quantify the effect of the cargo linker stiffness, the load, and the difference in intrinsic velocity on the synchronization of two coupled motor proteins. Herein, the mechanistic model and the new analysis techniques are demonstrated for the case of two coupled kinesin motors. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Physica D is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.physd.2009.01.005
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      – Code: eng
        Text: English
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        PageCount: 10
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      – SubjectFull: Kinesin
        Type: general
      – SubjectFull: Adenosine triphosphate
        Type: general
      – SubjectFull: Mechanical behavior of materials
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      – SubjectFull: Microtubules
        Type: general
      – SubjectFull: Brownian motion
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      – SubjectFull: Unsteady flow
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      – SubjectFull: Quantum perturbations
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      – SubjectFull: Transients (Dynamics)
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      – TitleFull: Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load
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            NameFull: Hendricks, Adam G.
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            NameFull: Epureanu, Bogdan I.
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            NameFull: Meyhöfer, Edgar
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              Text: Apr2009
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              Y: 2009
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