NADH Binds and stabilizes the 26S proteasomes independent of ATP

Peter Tsvetkov; Nadav Myers; Raz Eliav; Yaarit Adamovich; Tzachi Hagai; Julia Adler; Ami Navon; Yosef Shaul

doi:10.1074/jbc.M113.537175

NADH Binds and stabilizes the 26S proteasomes independent of ATP

Peter Tsvetkov, Nadav Myers, Raz Eliav, Yaarit Adamovich, Tzachi Hagai, Julia Adler, Ami Navon, Yosef Shaul^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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.

Original language	English
Pages (from-to)	11272-11281
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	289
Issue number	16
DOIs	https://doi.org/10.1074/jbc.M113.537175
State	Published - 18 Apr 2014
Externally published	Yes

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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.",

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AU - Tsvetkov, Peter

AU - Myers, Nadav

AU - Eliav, Raz

AU - Adamovich, Yaarit

AU - Hagai, Tzachi

AU - Adler, Julia

AU - Navon, Ami

AU - Shaul, Yosef

PY - 2014/4/18

Y1 - 2014/4/18

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AB - 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.

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NADH Binds and stabilizes the 26S proteasomes independent of ATP

Abstract

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