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  Uncovering global SUMOylation signaling networks in a site-specific manner

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, 21(10), 927-936. doi:10.1038/nsmb.2890.

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 Creators:
Hendriks, Ivo A.1, Author
D'Souza, Rochelle C. J.2, Author           
Yang, Bing1, Author
Verlaan-de Vries, Matty1, Author
Mann, Matthias2, Author           
Vertegaal, Alfred C. O.1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: NUCLEAR-PORE COMPLEX; KAPPA-B ACTIVATION; IN-VIVO; MASS-SPECTROMETRY; SUMO MODIFICATION; GENOTOXIC STRESS; UBIQUITIN; PROTEIN; REVEALS; PHOSPHORYLATION
 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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Language(s): eng - English
 Dates: 2014-10
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000342862000013
DOI: 10.1038/nsmb.2890
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 21 (10) Sequence Number: - Start / End Page: 927 - 936 Identifier: ISSN: 1545-9993