NADH Binds and stabilizes the 26S proteasomes independent of ATP

Abstract

Background: 26S proteasome complex is highly dependent on ATP. Results: NADH binds the proteasome via the Psmc1 subunit resulting in ATP-independent stabilization of the 26S proteasome complex, in vitro and in cells. Conclusion: NADH is a novel regulator of the 26S proteasome. Significance: NADH can maintain proteasomal integrity in the absence of ATP, linking cellular redox state to protein degradation. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.