Abstract
Cellular signaling pathways largely depend on the plasticity of multiprotein complexes. A central mechanism that assures the coordinated assembly and disassembly of protein complexes is the reversible post-translational modification of the individual components for example by phosphorylation, acetylation, or ubiquitylation. Accumulating evidence indicates that the small ubiquitin-related modifier (SUMO) system is another master organizer of protein complexes. Here, we will focus on the role of SUMO in the regulation of nuclear protein complexes that are involved in chromatin remodeling, double-strand break repair, and ribosome biogenesis. On the basis of these selected pathways, we will summarize current ideas of SUMO signaling, including the concept of group modification and the intersection of the ubiquitin and SUMO pathways.
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This work was supported by the “Deutsche Forschungsgemeinschaft” SPP1365. We thank all members of our lab for the critical reading and helpful discussions. We apologize to all authors whose original papers could not be cited due to space limitations.
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Nithya Raman and Arnab Nayak contributed equally to this manuscript.
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Raman, N., Nayak, A. & Muller, S. The SUMO system: a master organizer of nuclear protein assemblies. Chromosoma 122, 475–485 (2013). https://doi.org/10.1007/s00412-013-0429-6
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DOI: https://doi.org/10.1007/s00412-013-0429-6