Quality control of protein complex composition

Chris Padovani; Predrag Jevtić; Michael Rapé

doi:10.1016/j.molcel.2022.02.029

Quality control of protein complex composition

Mol Cell. 2022 Apr 21;82(8):1439-1450. doi: 10.1016/j.molcel.2022.02.029. Epub 2022 Mar 21.

Authors

Chris Padovani¹, Predrag Jevtić², Michael Rapé³

Affiliations

¹ Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
² Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.
³ Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA 94720, USA. Electronic address: mrape@berkeley.edu.

PMID: 35316660
DOI: 10.1016/j.molcel.2022.02.029

Abstract

Eukaryotic cells possess hundreds of protein complexes that contain multiple subunits and must be formed at the correct time and place during development. Despite specific assembly pathways, cells frequently encounter complexes with missing or aberrant subunits that can disrupt important signaling events. Cells, therefore, employ several ubiquitin-dependent quality control pathways that can prevent, correct, or degrade flawed complexes. In this review, we will discuss our emerging understanding of such quality control of protein complex composition.

Keywords: aneuploidy; dimerization quality control; orphan quality control; proteasome; quality control; ubiquitin; ubiquitylation.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Proteasome Endopeptidase Complex* / metabolism
Ubiquitin* / metabolism

Substances

Ubiquitin
Proteasome Endopeptidase Complex

Grants and funding

HHMI/Howard Hughes Medical Institute/United States