Moonlighting and pleiotropy within two regulators of the degradation machinery: The proteasome lid and the CSN

Elah Pick, Laylan Bramasole

Research output: Contribution to journalArticlepeer-review

Abstract

The distinction between pleiotrotic and moonlighting roles of proteins is challenging; however, this distinction may be clearer when it comes to multiprotein complexes. Two examples are the proteasome lid and the COP9 signalosome (CSN), which are twin enzymes with 1:1 paralogy between subunits. In each complex, one out of eight subunits harbours a JAMM/MPN+ metalloproteasemotif. Thismotif contributes the canonical activity of each complex: hydrolysis of covalently attached ubiquitin by Rpn11 in the proteasome lid and hydrolysis of ubiquitin-related 1 (Rub1/Nedd8) from Cullins by Csn5 in the CSN. In both complexes, executing this activity suggests pleiotropic effects and requires an assembled full complex. However, beyond canonical functions, both Rpn11 and Csn5 are involved in additional unique, complex-independent functions, herein referred to as moonlighting activities.

Original languageEnglish
Pages (from-to)1786-1791
Number of pages6
JournalBiochemical Society Transactions
Volume42
Issue number6
DOIs
StatePublished - 1 Dec 2014

Bibliographical note

Publisher Copyright:
© 2014 Biochemical Society.

Keywords

  • COP9 signalosome (CSN)
  • Moonlighting protein
  • Pleiotropy
  • Promiscuity
  • Proteasome lid
  • Protein complex

ASJC Scopus subject areas

  • Biochemistry

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