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SUMO pp 79–98Cite as

Identification and Characterization of SUMO-SIM Interactions

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1475))

Abstract

The covalent attachment of SUMO to lysine residues of cellular proteins serves as an important mechanism for the dynamic control of protein networks. SUMO conjugates typically mediate selected protein-protein interactions by binding to specific recognition modules. Identification of SUMO-binding proteins and the characterization of the binding motifs are key to understanding SUMO signaling. Here we describe two complementary approaches that are used to tackle these questions.

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Acknowledgements

The authors would like to acknowledge networking support by the Proteostasis COST action (BM1307) and the LOEWE Ub-Net. S.M. is funded by the DFG collaborative research centers SFB815 and SFB1177.

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Authors and Affiliations

  1. Institute of Biochemistry II, Goethe University, Medical School, Theodor-Stern-Kai 7, 60590, Frankfurt (Main), Germany

    Koraljka Husnjak, Jan Keiten-Schmitz & Stefan Müller

Authors
  1. Koraljka Husnjak
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  2. Jan Keiten-Schmitz
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  3. Stefan Müller
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Corresponding authors

Correspondence to Koraljka Husnjak or Stefan Müller .

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Editors and Affiliations

  1. INBIOMED, San Sebastian, Spain

    Manuel S. Rodriguez

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Husnjak, K., Keiten-Schmitz, J., Müller, S. (2016). Identification and Characterization of SUMO-SIM Interactions. In: Rodriguez, M. (eds) SUMO. Methods in Molecular Biology, vol 1475. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6358-4_6

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  • DOI: https://doi.org/10.1007/978-1-4939-6358-4_6

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-6356-0

  • Online ISBN: 978-1-4939-6358-4

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