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Uncovering global SUMOylation signaling networks in a site-specific manner

Open access
Hendriks, Ivo A, D'Souza, Rochelle C J, Yang, Bing, Verlaan-de Vries, Matty, Mann, Matthias, Vertegaal, Alfred C O·2014·Nature Structural & Molecular Biology

Abstract

SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution MS, we have studied global SUMOylation in human cells in a site-specific manner, identifying a total of >4,300 SUMOylation sites in >1,600 proteins. To our knowledge, this is the first time that >1,000 SUMOylation sites have been identified under standard growth conditions. We quantitatively studied SUMOylation dynamics in response to SUMO protease inhibition, proteasome inhibition and heat shock. Many SUMOylated lysines have previously been reported to be ubiquitinated, acetylated or methylated, thus indicating cross-talk between SUMO and other post-translational modifications. We identified 70 phosphorylation and four acetylation events in proximity to SUMOylation sites, and we provide evidence for acetylation-dependent SUMOylation of endogenous histone H3. SUMOylation regulates target proteins involved in all nuclear processes including transcription, DNA repair, chromatin remodeling, precursor-mRNA splicing and ribosome assembly.

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Metadata

Authors
Hendriks, I. A., D'Souza, R. C. J., Yang, B., Verlaan-de Vries, M., Mann, M., & Vertegaal, A. C. O.
Venue
Nature Structural & Molecular Biology
Published
2014-09-14
Volume
21
Issue
10
Pages
927-936
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2058434102
Cited by
486
References
2
FWCI
17.77
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Uncovering global SUMOylation signaling networks in a site-specific manner. https://app.cochat.ai/papers/10.1038/nsmb.2890
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Hendriks, I. A., D'Souza, R. C. J., Yang, B., Verlaan-de Vries, M., Mann, M., & Vertegaal, A. C. O. (2014). Uncovering global SUMOylation signaling networks in a site-specific manner. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2890

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