A proteomic study of SUMO-2 target proteins

Alfred C.O. Vertegaal, Stephen C. Ogg, Ellis Jaffray, Manuel S. Rodriguez, Ronald T. Hay, Jens S. Andersen, Matthias Mann, Angus I. Lamond

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Abstract

The SUMO family in vertebrates includes at least three distinct proteins (SUMO-1, -2, and -3) that are added as post-translational modifications to target proteins. A considerable number of SUMO-1 target proteins have been identified, but little is known about SUMO-2. A stable HeLa cell line expressing His6-tagged SUMO-2 was established and used to label and purify novel endogenous SUMO-2 target proteins. Tagged forms of SUMO-2 were functional and localized predominantly in the nucleus. His6-tagged SUMO-2 conjugates were affinity-purified from nuclear fractions and identified by mass spectrometry. Eight novel potential SUMO-2 target proteins were identified by at least two peptides. Three of these proteins, SART1, heterogeneous nuclear ribonucleoprotein (RNP) M, and the U5 small nuclear RNP 200-kDa helicase, play a role in RNA metabolism. SART1 and heterogeneous nuclear RNP M were both shown to be genuine SUMO targets, confirming the validity of the approach.

Original languageEnglish
Pages (from-to)33791-33798
Number of pages8
JournalJournal of Biological Chemistry
Volume279
Issue number32
DOIs
Publication statusPublished - 6 Aug 2004

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    Vertegaal, A. C. O., Ogg, S. C., Jaffray, E., Rodriguez, M. S., Hay, R. T., Andersen, J. S., Mann, M., & Lamond, A. I. (2004). A proteomic study of SUMO-2 target proteins. Journal of Biological Chemistry, 279(32), 33791-33798. https://doi.org/10.1074/jbc.M404201200