• 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

    ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    s41467-019-08686-0.pdf
    Size:
    5.098Mb
    Format:
    PDF
    Description:
    Final Published version
    Download
    Author
    Bertran, M Teresa
    Mouilleron, Stéphane
    Zhou, Yanxiang
    Bajaj, Rakhi
    Uliana, Federico
    Kumar, Ganesan Senthil
    van Drogen, Audrey
    Lee, Rebecca
    Banerjee, Jennifer J
    Hauri, Simon
    O'Reilly, Nicola
    Gstaiger, Matthias
    Page, Rebecca
    Peti, Wolfgang
    Tapon, Nicolas
    Show allShow less
    Affiliation
    Univ Arizona, Dept Chem & Biochem
    Issue Date
    2019-02-15
    
    Metadata
    Show full item record
    Publisher
    NATURE PUBLISHING GROUP
    Citation
    Bertran, M. T., Mouilleron, S., Zhou, Y., Bajaj, R., Uliana, F., Kumar, G. S., ... & O’Reilly, N. (2019). ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail. Nature communications, 10(1), 771.
    Journal
    NATURE COMMUNICATIONS
    Rights
    © The Author(s) 2019.
    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
    Serine/threonine phosphatases such as PP1 lack substrate specificity and associate with a large array of targeting subunits to achieve the requisite selectivity. The tumour suppressor ASPP (apoptosis-stimulating protein of p53) proteins associate with PP1 catalytic subunits and are implicated in multiple functions from transcriptional regulation to cell junction remodelling. Here we show that Drosophila ASPP is part of a multiprotein PP1 complex and that PP1 association is necessary for several in vivo functions of Drosophila ASPP. We solve the crystal structure of the human ASPP2/PP1 complex and show that ASPP2 recruits PP1 using both its canonical RVxF motif, which binds the PP1 catalytic domain, and its SH3 domain, which engages the PP1 C-terminal tail. The ASPP2 SH3 domain can discriminate between PP1 isoforms using an acidic specificity pocket in the n-Src domain, providing an exquisite mechanism where multiple motifs are used combinatorially to tune binding affinity to PP1.
    Note
    Open access journal
    ISSN
    2041-1723
    PubMed ID
    30770806
    DOI
    10.1038/s41467-019-08686-0
    Version
    Final published version
    Sponsors
    Francis Crick Institute; Cancer Research UK [FC001175]; UK Medical Research Council [FC001175]; Wellcome Trust [FC001175, 107885/Z/15/Z]; NIH [R01-GM098482, R01-NS091336]; European Union 7th Framework Programme SYBILLA (Systems Biology of T-Cell Activation); Innovative Medicines Initiative project ULTRA-DD [115766]
    Additional Links
    https://www.nature.com/articles/s41467-019-08686-0
    ae974a485f413a2113503eed53cd6c53
    10.1038/s41467-019-08686-0
    Scopus Count
    Collections
    UA Faculty Publications

    entitlement

    Related articles

    • Molecular mechanisms underlying the interaction of protein phosphatase-1c with ASPP proteins.
    • Authors: Skene-Arnold TD, Luu HA, Uhrig RG, De Wever V, Nimick M, Maynes J, Fong A, James MN, Trinkle-Mulcahy L, Moorhead GB, Holmes CF
    • Issue date: 2013 Feb 1
    • Inhibitory member of the apoptosis-stimulating proteins of the p53 family (iASPP) interacts with protein phosphatase 1 via a noncanonical binding motif.
    • Authors: Llanos S, Royer C, Lu M, Bergamaschi D, Lee WH, Lu X
    • Issue date: 2011 Dec 16
    • Leishmania PNUTS discriminates between PP1 catalytic subunits through an RVxF-ΦΦ-F motif and polymorphisms in the PP1 C-tail and catalytic domain.
    • Authors: Zhang Y, Sabatini R
    • Issue date: 2023 Dec
    • Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis.
    • Authors: Zhou Y, Millott R, Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
    • Issue date: 2019 Oct 1
    • Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators.
    • Authors: Gibbons JA, Weiser DC, Shenolikar S
    • Issue date: 2005 Apr 22
    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.