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

Weizmann Institute of Science

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

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

All Science Journal Classification (ASJC) codes

Molecular Biology
Biochemistry
Cell Biology

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10.1074/jbc.M113.537175

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title = "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.",

author = "Peter Tsvetkov and Nadav Myers and Raz Eliav and Yaarit Adamovich and Tzachi Hagai and Julia Adler and Ami Navon and Yosef Shaul",

note = "Israel Science Foundation [551/11]This work was supported by Israel Science Foundation Grant 551/11.",

year = "2014",

month = apr,

day = "18",

doi = "10.1074/jbc.M113.537175",

language = "الإنجليزيّة",

volume = "289",

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journal = "Journal of Biological Chemistry",

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T1 - NADH Binds and stabilizes the 26S proteasomes independent of ATP

AU - Tsvetkov, Peter

AU - Myers, Nadav

AU - Eliav, Raz

AU - Adamovich, Yaarit

AU - Hagai, Tzachi

AU - Adler, Julia

AU - Navon, Ami

AU - Shaul, Yosef

N1 - Israel Science Foundation [551/11]This work was supported by Israel Science Foundation Grant 551/11.

PY - 2014/4/18

Y1 - 2014/4/18

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84898966385&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.537175

DO - 10.1074/jbc.M113.537175

M3 - مقالة

SN - 0021-9258

VL - 289

SP - 11272

EP - 11281

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 16

ER -

NADH Binds and stabilizes the 26S proteasomes independent of ATP

Abstract

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