Formation of alternative proteasomes: Same lady, different cap?

Elah Pick, Tali S. Berman

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)389-393
Number of pages5
JournalFEBS Letters
Volume587
Issue number5
DOIs
StatePublished - 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

Fingerprint

Dive into the research topics of 'Formation of alternative proteasomes: Same lady, different cap?'. Together they form a unique fingerprint.

Cite this