System-wide changes to SUMO modifications in response to heat shock

Filip Golebiowski, Ivan Matic, Michael H. Tatham, Christian Cole, Yili Yin, Akihiro Nakamura, Juergen Cox, Geoffrey J. Barton, Matthias Mann, Ronald T. Hay (Lead / Corresponding author)

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    333 Citations (Scopus)

    Abstract

    Covalent conjugation of the small ubiquitin-like modifier (SUMO) proteins to target proteins regulates many important eukaryotic cellular mechanisms. Although the molecular consequences of the conjugation of SUMO proteins are relatively well understood, little is known about the cellular signals that regulate the modification of their substrates. Here, we show that SUMO-2 and SUMO-3 are required for cells to survive heat shock. Through quantitative labeling techniques, stringent purification of SUMOylated proteins, advanced mass spectrometric technology, and novel techniques of data analysis, we quantified heat shock-induced changes in the SUMOylation state of 766 putative substrates. In response to heat shock, SUMO was polymerized into polySUMO chains and redistributed among a wide range of proteins involved in cell cycle regulation; apoptosis; the trafficking, folding, and degradation of proteins; transcription; translation; and DNA replication, recombination, and repair. This comprehensive proteomic analysis of the substrates of a ubiquitin-like modifier (Ubl) identifies a pervasive role for SUMO proteins in the biologic response to hyperthermic stress.

    Original languageEnglish
    Article numberra24
    Number of pages12
    JournalScience Signaling
    Volume2
    Issue number72
    DOIs
    Publication statusPublished - 26 May 2009

    Keywords

    • UBIQUITIN-RELATED PROTEIN
    • MASS-SPECTROMETRY
    • IN-VIVO
    • QUANTITATIVE PROTEOMICS
    • MESSENGER-RNA
    • GENE ONTOLOGY
    • C-JUN
    • STRESS
    • SUMOYLATION
    • DATABASE

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