The ubiquitin proteoform problem. (August 2021)

• Record Type: Journal Article
• Authors: Deol, Kirandeep K.; Strieter, Eric R.
• Is Part Of: Current opinion in chemical biology. Volume 63(2021)
• Page Start: 95
• Page End: 104
• Publication Date: 2021-08
• Subjects: Proteoform -- Ubiquitin -- Ubiquitin chain -- Bottom-up proteomics -- Middle-down proteomics -- Top-down proteomics; Bioorganic chemistry -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Clinical biochemistry -- Periodicals; Biochemistry -- Periodicals; Chimie bio-organique -- Périodiques; Biologie -- Périodiques; 572.05
• DOI: 10.1016/j.cbpa.2021.02.015
• Languages: English
• ISSNs: 1367-5931

Abstract

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.