ASK1 Negatively Regulates the 26 S Proteasomeopen access
- Authors
- Um, Ji Won; Im, Eunju; Park, Joongkyu; Oh, Yohan; Min, Boram; Lee, Hyun Jung; Yoon, Jong Bok; Chung, Kwang Chul
- Issue Date
- Nov-2010
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.285, no.47, pp.36434 - 36446
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Volume
- 285
- Number
- 47
- Start Page
- 36434
- End Page
- 36446
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/173565
- DOI
- 10.1074/jbc.M110.133777
- ISSN
- 0021-9258
- Abstract
- The 26 S proteasome, composed of the 20 S core and 19 S regulatory particle, plays a central role in ubiquitin-dependent proteolysis. Disruption of this process contributes to the pathogenesis of the various diseases; however, the mechanisms underlying the regulation of 26 S proteasome activity remain elusive. Here, cell culture experiments and in vitro assays demonstrated that apoptosis signal-regulating kinase 1 (ASK1), a member of the MAPK kinase kinase family, negatively regulated 26 S proteasome activity. Immunoprecipitation/Western blot analyses revealed that ASK1 did not interact with 20 S catalytic core but did interact with ATPases making up the 19 S particle, which is responsible for recognizing polyubiquitinated proteins, unfolding them, and translocating them into the 20 S catalytic core in an ATP-dependent process. Importantly, ASK1 phosphorylated Rpt5, an AAA ATPase of the 19 S proteasome, and inhibited its ATPase activity, an effect that may underlie the ability of ASK1 to inhibit 26 S proteasome activity. The current findings point to a novel role for ASK1 in the regulation of 26 S proteasome and offer new strategies for treating human diseases caused by proteasome malfunction.
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