University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Interactome disassembly during apoptosis occurs independent of caspase cleavage

    Thumbnail
    Download
    published version (1.808Mb)

    Citations
    Scopus
    Web of Science
    Altmetric
    22
    22
    Author
    Scott, NE; Rogers, LD; Prudova, A; Brown, NF; Fortelny, N; Overall, CM; Foster, LJ
    Date
    2017-01-01
    Source Title
    Molecular Systems Biology
    Publisher
    WILEY
    University of Melbourne Author/s
    Scott, Nichollas
    Affiliation
    Microbiology and Immunology
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Scott, N. E., Rogers, L. D., Prudova, A., Brown, N. F., Fortelny, N., Overall, C. M. & Foster, L. J. (2017). Interactome disassembly during apoptosis occurs independent of caspase cleavage. MOLECULAR SYSTEMS BIOLOGY, 13 (1), https://doi.org/10.15252/msb.20167067.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/257655
    DOI
    10.15252/msb.20167067
    Abstract
    Protein-protein interaction networks (interactomes) define the functionality of all biological systems. In apoptosis, proteolysis by caspases is thought to initiate disassembly of protein complexes and cell death. Here we used a quantitative proteomics approach, protein correlation profiling (PCP), to explore changes in cytoplasmic and mitochondrial interactomes in response to apoptosis initiation as a function of caspase activity. We measured the response to initiation of Fas-mediated apoptosis in 17,991 interactions among 2,779 proteins, comprising the largest dynamic interactome to date. The majority of interactions were unaffected early in apoptosis, but multiple complexes containing known caspase targets were disassembled. Nonetheless, proteome-wide analysis of proteolytic processing by terminal amine isotopic labeling of substrates (TAILS) revealed little correlation between proteolytic and interactome changes. Our findings show that, in apoptosis, significant interactome alterations occur before and independently of caspase activity. Thus, apoptosis initiation includes a tight program of interactome rearrangement, leading to disassembly of relatively few, select complexes. These early interactome alterations occur independently of cleavage of these protein by caspases.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [45770]
    • Microbiology & Immunology - Research Publications [1555]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors