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dc.rights.licenseUsers may download and share copies with attribution in accordance with a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License. No commercial use or derivatives are permitted without the explicit approval of the author.
dc.contributorForth, Scott T.
dc.contributorGilbert, Susan P.
dc.contributorRoyer, Catherine Ann
dc.contributorSwank, Douglas M.
dc.contributorWang, Xing
dc.contributor.authorGaska, Ignas
dc.date.accessioned2021-11-03T09:23:40Z
dc.date.available2021-11-03T09:23:40Z
dc.date.created2021-07-07T15:42:34Z
dc.date.issued2020-12
dc.identifier.urihttps://hdl.handle.net/20.500.13015/2654
dc.descriptionDecember 2020
dc.descriptionSchool of Science
dc.description.abstractThe results indicated that the resistive forces generated by PRC1 crosslinked microtubule bundles scale with sliding velocity and the number of PRC1 within the bundle. Interestingly, the resistive forces measured were independent of microtubule bundle overlap length or PRC1 density within the bundle overlaps. From the data I argue that PRC1 acts as a mechanical dashpot indicating that the resistive forces generated by PRC1 ensembles scale proportionately to the velocity at which the bundle is being pulled apart. This behavior would generate higher resistance to fast acting motor proteins such as dynein while producing minimal resistance to slower acting motors such as kinesin-5 or kinesin-14 thereby playing an important role in the maintenance of a steady-state mitotic spindle.
dc.description.abstractThe eukaryotic mitotic spindle is a highly dynamic structure composed primarily of microtubules organized by motor and non-motor microtubule associated proteins (MAP’s). These protein-microtubule ensembles produce various pull-push forces at different rates as the spindle undergoes the multiple stages of mitosis. Strikingly, the spindle manages to maintain a steady-state throughout the entire mitotic process despite the various forces generated at multiple rates by microtubule-MAP interactions. The MAP PRC1 is one such protein which crosslinks microtubules in an antiparallel orientation within the central spindle and has been hypothesized to generate a resistive force to active motor protein microtubule sliding. The research presented within this document sought to recapitulate the activity of PRC1 and to quantify the hypothesized resistive forces. This was accomplished by reconstituting PRC1 crosslinked microtubule bundles and applying the techniques Total Internal Reflection Fluorescence Microscopy (TIRF) microscopy and optical trapping to measure the resistive forces using multiple parameters.
dc.language.isoENG
dc.publisherRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofRensselaer Theses and Dissertations Online Collection
dc.subjectBiology
dc.titleThe human microtubule crosslinking protein prc1 acts like a viscous dashpot to resist microtuble sliding during mitosis
dc.typeElectronic thesis
dc.typeThesis
dc.digitool.pid180458
dc.digitool.pid180459
dc.digitool.pid180460
dc.rights.holderThis electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
dc.description.degreePhD
dc.relation.departmentDept. of Biological Sciences


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