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Sci. Signal., 26 May 2009
Vol. 2, Issue 72, p. ra24
[DOI: 10.1126/scisignal.2000282]

RESEARCH

System-Wide Changes to SUMO Modifications in Response to Heat Shock

Filip Golebiowski1*, Ivan Matic2*, Michael H. Tatham1*, Christian Cole3, Yili Yin1, Akihiro Nakamura4, Jürgen Cox2, Geoffrey J. Barton3, Matthias Mann2, and Ronald T. Hay1{dagger}

1 Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
2 Department of Proteomics and Signal Transduction, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
3 College of Life Sciences Research, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
4 Department of Molecular and Cellular Pharmacology, Faculty of Medicine, Gunma University, Graduate School of Medicine, 3-39-22 Showa-Machi, Maebashi, Gunma 371-8511, Japan.

* These authors contributed equally to this work.

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.

{dagger} To whom correspondence should be addressed. E-mail: r.t.hay{at}dundee.ac.uk

Citation: F. Golebiowski, I. Matic, M. H. Tatham, C. Cole, Y. Yin, A. Nakamura, J. Cox, G. J. Barton, M. Mann, R. T. Hay, System-Wide Changes to SUMO Modifications in Response to Heat Shock. Sci. Signal. 2, ra24 (2009).

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