Abstract
The 26S proteasome is thought to be a homogenous complex, consisting of a 20S proteolytic core and a 19S regulatory particle that is required for its activation. Two groups have recently reported the activation of archeal 20S by a p97-related double-ring AAA+ ATPase complex, in a similar fashion to that reported for 19S. Since p97 is found in eukaryotes, the existence of a parallel setting in higher organisms is intriguing. Herein, we present supporting data and hypothesize that in eukaryotes, p97 and CSN form a promiscuous, hence hard-to-detect, "alternative cap", enabling the prompt and precise elimination of particular substrates.
Original language | English |
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Pages (from-to) | 389-393 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 587 |
Issue number | 5 |
DOIs | |
State | Published - 1 Mar 2013 |
Bibliographical note
Funding Information:We would like to thank the Israeli Science Foundation (grant no. EP355/10 for EP), for financial support of our studies.
Keywords
- 26S proteasome
- COP9 signalosome (CSN)
- Cullin RING E3 ligases
- P97
- Ubiquitin
- VAT
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology