Shared more. Cited more. Safe forever.
    • advanced search
    • submit works
    • about
    • help
    • contact us
    • login
    View Item 
    •   MOspace Home
    • University of Missouri-Columbia
    • Graduate School - MU Theses and Dissertations (MU)
    • Theses and Dissertations (MU)
    • Dissertations (MU)
    • 2008 Dissertations (MU)
    • 2008 MU dissertations - Access restricted to MU
    • View Item
    •   MOspace Home
    • University of Missouri-Columbia
    • Graduate School - MU Theses and Dissertations (MU)
    • Theses and Dissertations (MU)
    • Dissertations (MU)
    • 2008 Dissertations (MU)
    • 2008 MU dissertations - Access restricted to MU
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.
    advanced searchsubmit worksabouthelpcontact us

    Browse

    All of MOspaceCommunities & CollectionsDate IssuedAuthor/ContributorTitleIdentifierThesis DepartmentThesis AdvisorThesis SemesterThis CollectionDate IssuedAuthor/ContributorTitleIdentifierThesis DepartmentThesis AdvisorThesis Semester

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular AuthorsStatistics by Referrer

    Regulation of ceramide synthase 1 in cellular stress response

    Sridevi, Priya
    View/Open
    [PDF] public.pdf (2.426Kb)
    [PDF] short.pdf (56.37Kb)
    [PDF] research.pdf (18.43Mb)
    Date
    2008
    Format
    Thesis
    Metadata
    [+] Show full item record
    Abstract
    [ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] Ceramides are intimately involved in a wide range of cellular processes. In mammals, de novo ceramide synthesis is catalyzed by the 6 ceramide synthase enzymes, which are homologs of the yeast longevity assurance gene (lag). CerS1 catalyzes the synthesis of C18-ceramide, which has important roles in cell signaling, inflammation and apoptosis. In this study we show that CerS1 is a short-lived protein and that it undergoes stress-induced turnover in an ubiquitination and proteasome-dependent manner. This turnover is regulated by protein kinase C (PKC) and the p38 MAP kinase. This study also focuses on the stress-induced endoplasmic reticulum (ER) to Golgi translocation of the CerS1 protein. We show that CerS1 undergoes proteasome-dependent proteolytic cleavage under stress, as a result of which N-terminus CerS1 is degraded, while the Cterminus CerS1 translocates to the Golgi apparatus, also regulated in a PKC-dependent manner. Overall this study describes a novel regulatory mechanism for an important sphingolipid enzyme.
    URI
    https://hdl.handle.net/10355/6690
    https://doi.org/10.32469/10355/6690
    Degree
    Ph. D.
    Thesis Department
    Biological sciences (MU)
    Rights
    Access is limited to the campus of the University of Missouri--Columbia.
    Collections
    • 2008 MU dissertations - Access restricted to MU
    • Biological Sciences electronic theses and disserations (MU)

    Send Feedback
    hosted by University of Missouri Library Systems
     

     


    Send Feedback
    hosted by University of Missouri Library Systems