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Updated: May 6, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
Published on: January 29, 2018
Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains
Kirstin Keusekotten1, Veronika N Bade, Katrin Meyer-Teschendorf
1†Institute for Genetics, University of Cologne, 50674 Köln, Germany.
Abstract:
RNF4 (RING finger protein 4) is a STUbL [SUMO (small ubiquitin-related modifier)-targeted ubiquitin ligase] controlling PML (promyelocytic leukaemia) nuclear bodies, DNA double strand break repair and other nuclear functions. In the present paper, we describe that the sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.
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