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    Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes.

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    Author
    Liepe, J; Holzhütter, H-G; Bellavista, E; Kloetzel, PM; Stumpf, MPH; Mishto, M
    Date
    2015-09-22
    Source Title
    eLife
    Publisher
    eLife Sciences Publications, Ltd
    University of Melbourne Author/s
    Stumpf, Michael
    Affiliation
    School of BioSciences
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Liepe, J., Holzhütter, H. -G., Bellavista, E., Kloetzel, P. M., Stumpf, M. P. H. & Mishto, M. (2015). Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes.. Elife, 4, pp.e07545-. https://doi.org/10.7554/eLife.07545.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253453
    DOI
    10.7554/eLife.07545
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4611054
    Abstract
    Proteasomal protein degradation is a key determinant of protein half-life and hence of cellular processes ranging from basic metabolism to a host of immunological processes. Despite its importance the mechanisms regulating proteasome activity are only incompletely understood. Here we use an iterative and tightly integrated experimental and modelling approach to develop, explore and validate mechanistic models of proteasomal peptide-hydrolysis dynamics. The 20S proteasome is a dynamic enzyme and its activity varies over time because of interactions between substrates and products and the proteolytic and regulatory sites; the locations of these sites and the interactions between them are predicted by the model, and experimentally supported. The analysis suggests that the rate-limiting step of hydrolysis is the transport of the substrates into the proteasome. The transport efficiency varies between human standard- and immuno-proteasomes thereby impinging upon total degradation rate and substrate cleavage-site usage.

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