Analysis of Cooperative Behavior in Multiple Kinesins Motor Protein Transport by Varying Structural and Chemical Properties

Simple item page
dc.citation.firstpage38en_US
dc.citation.issueNumber1en_US
dc.citation.journalTitleCellular and Molecular Bioengineeringen_US
dc.citation.lastpage47en_US
dc.citation.volumeNumber6en_US
dc.contributor.authorUppulury, Karthiken_US
dc.contributor.authorEfremov, Artem K.en_US
dc.contributor.authorDriver, Jonathan W.en_US
dc.contributor.authorJamison, D. Kennethen_US
dc.contributor.authorDiehl, Michael R.en_US
dc.contributor.authorKolomeisky, Anatoly B.en_US
dc.date.accessioned2014-10-08T21:25:36Zen_US
dc.date.available2014-10-08T21:25:36Zen_US
dc.date.issued2013en_US
dc.description.abstractIntracellular transport is a fundamental biological process during which cellular materials are driven by enzymatic molecules called motor proteins. Recent optical trapping experiments and theoretical analysis have uncovered many features of cargo transport by multiple kinesin motor protein molecules under applied loads. These studies suggest that kinesins cooperate negatively under typical transport conditions, although some productive cooperation could be achieved under higher applied loads. However, the microscopic origins of this complex behavior are still not well understood. Using a discrete-state stochastic approach we analyze factors that affect the cooperativity among kinesin motors during cargo transport. Kinesin cooperation is shown to be largely unaffected by the structural and mechanical parameters of a multiple motor complex connected to a cargo, but much more sensitive to biochemical parameters affecting motor-filament affinities. While such behavior suggests the net negative cooperative responses of kinesins will persist across a relatively wide range of cargo types, it is also shown that the rates with which cargo velocities relax in time upon force perturbations are influenced by structural factors that affect the free energies of and load distributions within a multiple kinesin complex. The implications of these later results on transport phenomena where loads change temporally, as in the case of bidirectional transport, are discussed.en_US
dc.identifier.citationUppulury, Karthik, Efremov, Artem K., Driver, Jonathan W., et al.. "Analysis of Cooperative Behavior in Multiple Kinesins Motor Protein Transport by Varying Structural and Chemical Properties." <i>Cellular and Molecular Bioengineering,</i> 6, no. 1 (2013) Springer: 38-47. http://dx.doi.org/10.1007/s12195-012-0260-9.en_US
dc.identifier.doihttp://dx.doi.org/10.1007/s12195-012-0260-9en_US
dc.identifier.urihttps://hdl.handle.net/1911/77454en_US
dc.language.isoengen_US
dc.publisherSpringeren_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer.en_US
dc.subject.keywordintracellular transporten_US
dc.subject.keywordkinesinen_US
dc.subject.keywordcooperativityen_US
dc.titleAnalysis of Cooperative Behavior in Multiple Kinesins Motor Protein Transport by Varying Structural and Chemical Propertiesen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
nihms424171.pdf
Size:
1.03 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Faculty Publications
Bioengineering Publications
Chemistry Publications