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Proposed model for regulation of TDP2 by Ubiquitin and SUMO2/3. (A) TDP2 forms a compact state where the UBA domain decreases catalytic activity, or an extended conformation with increased catalytic activity. Binding to poly-Ubiquitin stabilizes the extended and active conformation. Proteins that are K63 (or K27) poly-ubiquitinated can function as regulatory signals that increase TDP2 hydrolase activity on 5′-Y DNA.
