The ubiquitin proteoform problem

Kirandeep K Deol; Eric R Strieter

doi:10.1016/j.cbpa.2021.02.015

The ubiquitin proteoform problem

Curr Opin Chem Biol. 2021 Aug:63:95-104. doi: 10.1016/j.cbpa.2021.02.015. Epub 2021 Apr 1.

Authors

Kirandeep K Deol¹, Eric R Strieter²

Affiliations

¹ Department of Chemistry, University of Massachusetts, Amherst, MA, 01003, USA.
² Department of Chemistry, University of Massachusetts, Amherst, MA, 01003, USA; Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, 01003, USA.

Abstract

The diversity of ubiquitin modifications is immense. A protein can be monoubiquitylated, multi-monoubiquitylated, and polyubiquitylated with chains varying in size and shape. Ubiquitin itself can be adorned with other ubiquitin-like proteins and smaller functional groups. Considering different combinations of post-translational modifications can give rise to distinct biological outcomes, characterizing ubiquitylated proteoforms of a given protein is paramount. In this Opinion, we review recent advances in detecting and quantifying various ubiquitin proteoforms using mass spectrometry.

Keywords: Bottom-up proteomics; Middle-down proteomics; Proteoform; Top-down proteomics; Ubiquitin; Ubiquitin chain.

Publication types

Research Support, N.I.H., Extramural
Review

MeSH terms

Binding Sites
Humans
Lysine / chemistry
Mass Spectrometry
Protein Conformation
Protein Processing, Post-Translational
Proteome / chemistry*
Proteomics
Substrate Specificity
Ubiquitin / chemistry*
Ubiquitination

Substances

Proteome
Ubiquitin
Lysine

Grants and funding

R01 GM110543/GM/NIGMS NIH HHS/United States