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Coupling between motorproteins determines dynamic behaviors of motorproteinassemblies
Transport of intracellular cargos by multiple microtubule motorproteins is believed to be a common and significant phenomenon in vivo , yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determ...
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Published in: | Physical chemistry chemical physics : PCCP 2010-08, Vol.12 (35), p.1398-145 |
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creator | Driver, Jonathan W Rogers, Arthur R Jamison, D. Kenneth Das, Rahul K Kolomeisky, Anatoly B Diehl, Michael R |
description | Transport of intracellular cargos by multiple microtubule motorproteins is believed to be a common and significant phenomenon
in vivo
, yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determining how grouping motors affect their association with microtubules and stepping rates, and hence, cargo run lengths and velocities. We examined this problem using a discrete state transition rate model of collective transport. This model accounts for the structural and mechanical properties in binding/unbinding and stepping transitions between distinct microtubule-bound configurations of a multiple motor system. In agreement with previous experiments that examine the dynamics of two coupled kinesin-1 motors, the energetic costs associated with deformations of mechanical linkages within a multiple motorassembly are found to reduce the system's overall microtubule affinity, producing attenuated mean cargo run lengths compared to cases where motors are assumed to function independently. With our present treatment, this attenuation largely stems from reductions in the microtubule binding rate and occurs even when mechanical coupling between motors is weak. Thus, our model suggests that, at least for a variety of kinesin-dependent transport processes, the net 'gains' obtained by grouping motors together may be smaller than previously expected.
A microscopic model of collective motor dynamics demonstrates the influence of structural properties of multiple motor systems on their net collective behaviors. |
doi_str_mv | 10.1039/c0cp00117a |
format | article |
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in vivo
, yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determining how grouping motors affect their association with microtubules and stepping rates, and hence, cargo run lengths and velocities. We examined this problem using a discrete state transition rate model of collective transport. This model accounts for the structural and mechanical properties in binding/unbinding and stepping transitions between distinct microtubule-bound configurations of a multiple motor system. In agreement with previous experiments that examine the dynamics of two coupled kinesin-1 motors, the energetic costs associated with deformations of mechanical linkages within a multiple motorassembly are found to reduce the system's overall microtubule affinity, producing attenuated mean cargo run lengths compared to cases where motors are assumed to function independently. With our present treatment, this attenuation largely stems from reductions in the microtubule binding rate and occurs even when mechanical coupling between motors is weak. Thus, our model suggests that, at least for a variety of kinesin-dependent transport processes, the net 'gains' obtained by grouping motors together may be smaller than previously expected.
A microscopic model of collective motor dynamics demonstrates the influence of structural properties of multiple motor systems on their net collective behaviors.</description><identifier>ISSN: 1463-9076</identifier><identifier>EISSN: 1463-9084</identifier><identifier>DOI: 10.1039/c0cp00117a</identifier><language>eng</language><subject>Attenuation ; Binding ; Dynamical systems ; Dynamics ; Joining ; Motors ; Stems ; Transport</subject><ispartof>Physical chemistry chemical physics : PCCP, 2010-08, Vol.12 (35), p.1398-145</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Driver, Jonathan W</creatorcontrib><creatorcontrib>Rogers, Arthur R</creatorcontrib><creatorcontrib>Jamison, D. Kenneth</creatorcontrib><creatorcontrib>Das, Rahul K</creatorcontrib><creatorcontrib>Kolomeisky, Anatoly B</creatorcontrib><creatorcontrib>Diehl, Michael R</creatorcontrib><title>Coupling between motorproteins determines dynamic behaviors of motorproteinassemblies</title><title>Physical chemistry chemical physics : PCCP</title><description>Transport of intracellular cargos by multiple microtubule motorproteins is believed to be a common and significant phenomenon
in vivo
, yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determining how grouping motors affect their association with microtubules and stepping rates, and hence, cargo run lengths and velocities. We examined this problem using a discrete state transition rate model of collective transport. This model accounts for the structural and mechanical properties in binding/unbinding and stepping transitions between distinct microtubule-bound configurations of a multiple motor system. In agreement with previous experiments that examine the dynamics of two coupled kinesin-1 motors, the energetic costs associated with deformations of mechanical linkages within a multiple motorassembly are found to reduce the system's overall microtubule affinity, producing attenuated mean cargo run lengths compared to cases where motors are assumed to function independently. With our present treatment, this attenuation largely stems from reductions in the microtubule binding rate and occurs even when mechanical coupling between motors is weak. Thus, our model suggests that, at least for a variety of kinesin-dependent transport processes, the net 'gains' obtained by grouping motors together may be smaller than previously expected.
A microscopic model of collective motor dynamics demonstrates the influence of structural properties of multiple motor systems on their net collective behaviors.</description><subject>Attenuation</subject><subject>Binding</subject><subject>Dynamical systems</subject><subject>Dynamics</subject><subject>Joining</subject><subject>Motors</subject><subject>Stems</subject><subject>Transport</subject><issn>1463-9076</issn><issn>1463-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp90E1LxDAQBuAgCq6rF-9CvXmp5qv5OEpxVVjwsp5Lmk400jY16Sr77w2sKF48zTvDwzAMQucEXxPM9I3FdsKYEGkO0IJwwUqNFT_8yVIco5OU3nBGFWEL9FyH7dT78aVoYf4EGIshzCFOMczgx1R0MEMc_Ag57kYzeJvhq_nwIaYiuD_apARD23tIp-jImT7B2Xddos3qblM_lOun-8f6dl1OiriSsooqU3FjBROStq3VFeeKO2hbiXlumO6AdkobRqjTwmGWpxJ3olOCaLZEV_u1-YD3LaS5GXyy0PdmhLBNDZFEaSoJx5le7mlMtpmiH0zcNb_faqbOZXPxn2FfshNqLA</recordid><startdate>20100825</startdate><enddate>20100825</enddate><creator>Driver, Jonathan W</creator><creator>Rogers, Arthur R</creator><creator>Jamison, D. Kenneth</creator><creator>Das, Rahul K</creator><creator>Kolomeisky, Anatoly B</creator><creator>Diehl, Michael R</creator><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20100825</creationdate><title>Coupling between motorproteins determines dynamic behaviors of motorproteinassemblies</title><author>Driver, Jonathan W ; Rogers, Arthur R ; Jamison, D. Kenneth ; Das, Rahul K ; Kolomeisky, Anatoly B ; Diehl, Michael R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p81f-23528a54ac63672bbc954484febb70495439de2d89a312f96f0349570d6d86193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Attenuation</topic><topic>Binding</topic><topic>Dynamical systems</topic><topic>Dynamics</topic><topic>Joining</topic><topic>Motors</topic><topic>Stems</topic><topic>Transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Driver, Jonathan W</creatorcontrib><creatorcontrib>Rogers, Arthur R</creatorcontrib><creatorcontrib>Jamison, D. Kenneth</creatorcontrib><creatorcontrib>Das, Rahul K</creatorcontrib><creatorcontrib>Kolomeisky, Anatoly B</creatorcontrib><creatorcontrib>Diehl, Michael R</creatorcontrib><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Physical chemistry chemical physics : PCCP</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Driver, Jonathan W</au><au>Rogers, Arthur R</au><au>Jamison, D. Kenneth</au><au>Das, Rahul K</au><au>Kolomeisky, Anatoly B</au><au>Diehl, Michael R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Coupling between motorproteins determines dynamic behaviors of motorproteinassemblies</atitle><jtitle>Physical chemistry chemical physics : PCCP</jtitle><date>2010-08-25</date><risdate>2010</risdate><volume>12</volume><issue>35</issue><spage>1398</spage><epage>145</epage><pages>1398-145</pages><issn>1463-9076</issn><eissn>1463-9084</eissn><abstract>Transport of intracellular cargos by multiple microtubule motorproteins is believed to be a common and significant phenomenon
in vivo
, yet signatures of the microscopic dynamics of multiple motor systems are only now beginning to be resolved. Understanding these mechanisms largely depends on determining how grouping motors affect their association with microtubules and stepping rates, and hence, cargo run lengths and velocities. We examined this problem using a discrete state transition rate model of collective transport. This model accounts for the structural and mechanical properties in binding/unbinding and stepping transitions between distinct microtubule-bound configurations of a multiple motor system. In agreement with previous experiments that examine the dynamics of two coupled kinesin-1 motors, the energetic costs associated with deformations of mechanical linkages within a multiple motorassembly are found to reduce the system's overall microtubule affinity, producing attenuated mean cargo run lengths compared to cases where motors are assumed to function independently. With our present treatment, this attenuation largely stems from reductions in the microtubule binding rate and occurs even when mechanical coupling between motors is weak. Thus, our model suggests that, at least for a variety of kinesin-dependent transport processes, the net 'gains' obtained by grouping motors together may be smaller than previously expected.
A microscopic model of collective motor dynamics demonstrates the influence of structural properties of multiple motor systems on their net collective behaviors.</abstract><doi>10.1039/c0cp00117a</doi><tpages>8</tpages></addata></record> |
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source | Royal Society of Chemistry |
subjects | Attenuation Binding Dynamical systems Dynamics Joining Motors Stems Transport |
title | Coupling between motorproteins determines dynamic behaviors of motorproteinassemblies |
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