SUMO Conjugation - a mechanistic view

Pichler, Andreas; Fatouros, Chronis; Lee, Heekyoung; Eisenhardt, Nathalie

doi:10.1515/bmc-2016-0030

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SUMO Conjugation - a mechanistic view

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Pichler, Andreas
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Fatouros, Chronis
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Lee, Heekyoung
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Eisenhardt, Nathalie
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Pichler, A., Fatouros, C., Lee, H., & Eisenhardt, N. (2017). SUMO Conjugation - a mechanistic view. Biomolecular Concepts, 8, 13-36. doi:10.1515/bmc-2016-0030.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-8605-4

Abstract

The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate. We focus on the interplay of the E1, E2 and E3 enzymes and discuss how specificity could be achieved given the limited number of conjugating enzymes and the thousands of substrates.