Ubiquitin-interacting motifs confer full catalytic activity, but not ubiquitin chain substrate specificity, to deubiquitinating enzyme USP37

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Abstract

Background: The role of ubiquitin-interacting motifs (UIMs) in the deubiquitinating enzyme USP37 is unknown. Results: Inactivation of the UIMs in USP37 resulted in lower isopeptidase activity toward ubiquitin chains. Conclusion: The UIMs in USP37 are required for the full catalytic activity of the enzyme. Significance: This study reveals a novel mechanism to increase the catalytic activity of deubiquitinating enzymes. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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Tanno, H., Shigematsu, T., Nishikawa, S., Hayakawa, A., Denda, K., Tanaka, T., & Komada, M. (2014). Ubiquitin-interacting motifs confer full catalytic activity, but not ubiquitin chain substrate specificity, to deubiquitinating enzyme USP37. Journal of Biological Chemistry, 289(4), 2415–2423. https://doi.org/10.1074/jbc.M113.528372

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