Targeting of SUMO substrates to a Cdc48–Ufd1–Npl4 segregase and STUbL pathway in fission yeast

Julie Bonne Køhler, Triin Tammsalu, Maria Mønster Jørgensen, Nana Steen, Ronald Thomas Hay () and Geneviève Thon ()
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Julie Bonne Køhler: University of Copenhagen, Ole MaalÃes vej 5, Copenhagen DK-2200, Denmark
Triin Tammsalu: Centre for Gene Regulation and Expression, Sir James Black Centre, College of Life Sciences, University of Dundee
Maria Mønster Jørgensen: University of Copenhagen, Ole MaalÃes vej 5, Copenhagen DK-2200, Denmark
Nana Steen: University of Copenhagen, Ole MaalÃes vej 5, Copenhagen DK-2200, Denmark
Ronald Thomas Hay: Centre for Gene Regulation and Expression, Sir James Black Centre, College of Life Sciences, University of Dundee
Geneviève Thon: University of Copenhagen, Ole MaalÃes vej 5, Copenhagen DK-2200, Denmark

Nature Communications, 2015, vol. 6, issue 1, 1-14

Abstract: Abstract In eukaryotes, the conjugation of proteins to the small ubiquitin-like modifier (SUMO) regulates numerous cellular functions. A proportion of SUMO conjugates are targeted for degradation by SUMO-targeted ubiquitin ligases (STUbLs) and it has been proposed that the ubiquitin-selective chaperone Cdc48/p97-Ufd1-Npl4 facilitates this process. However, the extent to which the two pathways overlap, and how substrates are selected, remains unknown. Here we address these questions in fission yeast through proteome-wide analyses of SUMO modification sites. We identify over a thousand sumoylated lysines in a total of 468 proteins and quantify changes occurring in the SUMO modification status when the STUbL or Ufd1 pathways are compromised by mutations. The data suggest the coordinated processing of several classes of SUMO conjugates, many dynamically associated with centromeres or telomeres. They provide new insights into subnuclear organization and chromosome biology, and, altogether, constitute an extensive resource for the molecular characterization of SUMO function and dynamics.

Date: 2015
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DOI: 10.1038/ncomms9827

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