The Role of Multifilament Structures and Lateral Interactions in Dynamics of Cytoskeleton Proteins and Assemblies

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dc.citation.firstpage4653
dc.citation.issueNumber13
dc.citation.journalTitleThe Journal of Physical Chemistry B
dc.citation.lastpage4661
dc.citation.volumeNumber119
dc.contributor.authorLi, Xin
dc.contributor.authorKolomeisky, Anatoly B.
dc.contributor.orgCenter for Theoretical Biological Physics
dc.date.accessioned2015-06-15T18:57:49Z
dc.date.available2015-06-15T18:57:49Z
dc.date.issued2015
dc.description.abstractMicrotubules and actin filaments are biopolymer molecules that are major components of cytoskeleton networks in biological cells. They play important roles in supporting fundamental cellular processes such as cell division, signaling, locomotion, and intracellular transport. In cells, cytoskeleton proteins function under nonequilibrium conditions that are powered by hydrolysis of adenosine triphosphate (ATP) or guanosine triphosphate (GTP) molecules attached to them. Although these biopolymers are critically important for all cellular processes, the mechanisms that govern their complex dynamics and force generation remain not well explained. One of the most difficult fundamental issues is to understand how different components of cytoskeleton proteins interact together. We develop an approximate theoretical approach for analyzing complex processes in cytoskeleton proteins that takes into account the multifilament structure, lateral interactions between parallel protofilaments, and the most relevant biochemical transitions during the biopolymer growth. It allows us to fully evaluate collective dynamic properties of cytoskeleton filaments as well as the effect of external forces on them. It is found that for the case of strong lateral interactions the stall force of the multifilament protein is a linear function of the number of protofilaments. However, for weak lateral interactions, deviations from the linearity are observed. We also show that stall forces, mean velocities, and dispersions are increasing functions of the lateral interactions. Physicalﾖchemical explanations of these phenomena are presented. Our theoretical predictions are supported by extensive Monte Carlo computer simulations.
dc.identifier.citationLi, Xin and Kolomeisky, Anatoly B.. "The Role of Multifilament Structures and Lateral Interactions in Dynamics of Cytoskeleton Proteins and Assemblies." <i>The Journal of Physical Chemistry B,</i> 119, no. 13 (2015) American Chemical Society: 4653-4661. http://dx.doi.org/10.1021/acs.jpcb.5b01219.
dc.identifier.doihttp://dx.doi.org/10.1021/acs.jpcb.5b01219
dc.identifier.urihttps://hdl.handle.net/1911/80752
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by the American Chemical Society
dc.subject.keywordcytoskeleton assembly
dc.subject.keywordhydrolysis
dc.subject.keywordlateral interactions
dc.subject.keywordstall force
dc.titleThe Role of Multifilament Structures and Lateral Interactions in Dynamics of Cytoskeleton Proteins and Assemblies
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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