• Login
    View Item 
    •   Home
    • UA Faculty Research
    • UA Faculty Publications
    • View Item
    •   Home
    • UA Faculty Research
    • UA Faculty Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UA Campus RepositoryCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournalThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournal

    My Account

    LoginRegister

    About

    AboutUA Faculty PublicationsUA DissertationsUA Master's ThesesUA Honors ThesesUA PressUA YearbooksUA CatalogsUA Libraries

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Changes to the TDP-43 and FUS Interactomes Induced by DNA Damage

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    acs.jproteome.9b00575.pdf
    Size:
    2.231Mb
    Format:
    PDF
    Description:
    Final Published Version
    Download
    Author
    Kawaguchi, Tetsuya
    Rollins, Matthew G.
    Moinpour, Mahta
    Morera, Andres A.
    Ebmeier, Christopher C.
    Old, William M.
    Schwartz, Jacob C.
    Affiliation
    Univ Arizona, Dept Mol & Cellular Biol
    Univ Arizona, Dept Chem & Biochem
    Issue Date
    2019-11-06
    Keywords
    TDP-43
    FUS
    DNA damage repair
    transcription
    amyotrophic lateral sclerosis
    frontal temporal dementia
    
    Metadata
    Show full item record
    Publisher
    AMER CHEMICAL SOC
    Citation
    J. Proteome Res. 2020, 19, 1, 360-370
    Journal
    JOURNAL OF PROTEOME RESEARCH
    Rights
    Copyright © 2019 American Chemical Society
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    The RNA-binding proteins TDP-43 and FUS are tied as the thirdleading known genetic cause for amyotrophic lateral sclerosis (ALS), and TDP-43proteopathies are found in nearly all ALS patients. Both the natural function andcontribution to pathology for TDP-43 remain unclear. The intersection offunctions between TDP-43 and FUS can focus attention for those natural functionsmostly likely to be relevant to disease. Here, we compare the role played by TDP-43 and FUS, maintaining chromatin stability for dividing HEK293T cells. We alsodetermine and compare the interactomes of TDP-43 and FUS, quantitatingchanges in those before and after DNA damage. Finally, selected interactions withknown importance to DNA damage repair were validated by co-immunoprecipi-tation assays. This study uncovered TDP-43 and FUS binding to several factorsimportant to DNA repair mechanisms that can be replication-dependent,-independent, or both. These results provide further evidence that TDP-43 has an important role in DNA stability andprovide new ways that TDP-43 can bind to the machinery that guards DNA integrity in cells.
    Note
    Open access article
    ISSN
    1535-3893
    DOI
    10.1021/acs.jproteome.9b00575
    Version
    Final published version
    Sponsors
    This work was funded by the National Institute of Health [NS082376] to J.C.S. and by a DARPA cooperative agreement grant [13-34-RTA-FP-007] to W.M.O. Research was also supported by the Office of the Director, National Institutes of Health of the National Institutes of Health under award number S10OD013237.
    ae974a485f413a2113503eed53cd6c53
    10.1021/acs.jproteome.9b00575
    Scopus Count
    Collections
    UA Faculty Publications

    entitlement

     
    The University of Arizona Libraries | 1510 E. University Blvd. | Tucson, AZ 85721-0055
    Tel 520-621-6442 | repository@u.library.arizona.edu
    DSpace software copyright © 2002-2017  DuraSpace
    Quick Guide | Contact Us | Send Feedback
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.