• About
    • Login
    View Item 
    •   Institutional Repository Home
    • Electronic Theses and Dissertations
    • Electronic Theses and Dissertations
    • View Item
    •   Institutional Repository Home
    • Electronic Theses and Dissertations
    • Electronic Theses and Dissertations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of Institutional RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    Myosin-1d expression and dynamics in polarized cells

    Benesh, Andrew Eugene
    : https://etd.library.vanderbilt.edu/etd-12022011-134648
    http://hdl.handle.net/1803/15023
    : 2011-12-12

    Abstract

    Class I myosins are monomeric actin-binding, ATP hydrolyzing molecular motors that are expressed in a variety of cell types, and function at the membrane-actin interface. Myosin-1d, one of eight vertebrate class I myosins, is expressed in polarized cells of the small intestine and nervous system, but subcellular localization and function for the motor remains largely unexplored. Intriguingly, myosin-1d is coexpressed in epithelial cells of the small intestine with myosin-a, where both motors target to the well-defined apical actin array of the brush border. However, how similar class I motors compartmentalize subcellularly is unknown, and raises the question of functional overlap. Interestingly, we found that myosin-1d and myosin1a exhibit differential localization and this partitioning can be explained by differential dynamics. Moreover, myosin-1d redistributes along the microvillar actin bundle in the absence of myosin-1a in MYO1A knockout animals. This suggests that class I myosins do have unique functions in wildtype, but may compensate for loss of activity. Interestingly, our data demonstrates that myosin-1d has a different subcellular localization in the nervous system. In these polarized cells, myosin-1d exhibits a punctate distribution in neuronal dendrites, cell bodies, and axons. We observed prominent expression in Purkinje cells and a subset of granule cells, with both patterns developmentally regulated. However, myosin-1d was not detectable in oligodendrocytes during early development. In the PNS, we observed that myosin-1d is present in neurons, and myelinating Schwann cells. This suggests a differential role for the motor in myelinating cells between the two nervous systems. Our studies also revealed that myosin-1d interacts with aspartoacylase, a catalytic enzyme involved in fatty acid synthesis that is widely expressed in similar polarized cells as myosin-1d. Together, these studies suggest that myosin-1d has distinct localization patterns in different polarized cell types, but may modulate aspartoacylase activity.
    Show full item record

    Files in this item

    Icon
    Name:
    AEBDISSERTATIONFORSUBMISSION.pdf
    Size:
    106.7Mb
    Format:
    PDF
    View/Open

    This item appears in the following collection(s):

    • Electronic Theses and Dissertations

    Connect with Vanderbilt Libraries

    Your Vanderbilt

    • Alumni
    • Current Students
    • Faculty & Staff
    • International Students
    • Media
    • Parents & Family
    • Prospective Students
    • Researchers
    • Sports Fans
    • Visitors & Neighbors

    Support the Jean and Alexander Heard Libraries

    Support the Library...Give Now

    Gifts to the Libraries support the learning and research needs of the entire Vanderbilt community. Learn more about giving to the Libraries.

    Become a Friend of the Libraries

    Quick Links

    • Hours
    • About
    • Employment
    • Staff Directory
    • Accessibility Services
    • Contact
    • Vanderbilt Home
    • Privacy Policy