Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

Ivan Matic, Joost Schimmel, Ivor .A. Hendriks, Maria A. van Santen, Frans van de Rijke, Hans van Dam, Florian Gnad, Matthias Mann (Lead / Corresponding author), Alfred C. O. Vertegaal (Lead / Corresponding author)

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    Abstract

    Reversible protein modification by small ubiquitin-like modifiers (SUMOs) is critical for eukaryotic life. Mass spectrometry-based proteomics has proven effective at identifying hundreds of potential SUMO target proteins. However, direct identification of SUMO acceptor lysines in complex samples by mass spectrometry is still very challenging. We have developed a generic method for the identification of SUMO acceptor lysines in target proteins. We have identified 103 SUMO-2 acceptor lysines in endogenous target proteins. Of these acceptor lysines, 76 are situated in the SUMOylation consensus site [VILMFPC]KxE. Interestingly, eight sites fit the inverted SUMOylation consensus motif [ED]xK[VILFP]. In addition, we found direct mass spectrometric evidence for crosstalk between SUMOylation and phosphorylation with a preferred spacer between the SUMOylated lysine and the phosphorylated serine of four residues. In 16 proteins we identified a hydrophobic cluster SUMOylation motif (HCSM). SUMO conjugation of RanGAP1 and ZBTB1 via HCSMs is remarkably efficient.
    Original languageEnglish
    Pages (from-to)641-652
    Number of pages12
    JournalMolecular Cell
    Volume39
    Issue number4
    DOIs
    Publication statusPublished - 27 Aug 2010

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    Matic, I., Schimmel, J., Hendriks, I. . A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., & Vertegaal, A. C. O. (2010). Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Molecular Cell, 39(4), 641-652. https://doi.org/10.1016/j.molcel.2010.07.026