Format

Send to

Choose Destination
Trends Biochem Sci. 2017 Nov;42(11):873-886. doi: 10.1016/j.tibs.2017.09.002. Epub 2017 Sep 22.

The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy.

Author information

1
Protein Metabolism Medical Research Center and Department of Biomedical Sciences, College of Medicine, Seoul National University, Seoul 110-799, Korea; Ischemic/Hypoxic Disease Institute, College of Medicine, Seoul National University, Seoul 110-799, Korea. Electronic address: yok5@snu.ac.kr.
2
Protein Metabolism Medical Research Center and Department of Biomedical Sciences, College of Medicine, Seoul National University, Seoul 110-799, Korea; Technion Integrated Cancer Center (TICC), The Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, Haifa 31096, Israel. Electronic address: aaroncie@technion.ac.il.

Abstract

The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate (monoubiquitination), ubiquitin can itself be ubiquitinated on any of its seven lysine (Lys) residues or its N-terminal methionine (Met1). A single ubiquitin polymer may contain mixed linkages and/or two or more branches. In addition, ubiquitin can be conjugated with ubiquitin-like modifiers such as SUMO or small molecules such as phosphate. The diverse ways to assemble ubiquitin chains provide countless means to modulate biological processes. We overview here the complexity of the ubiquitin code, with an emphasis on the emerging role of linkage-specific degradation signals (degrons) in the ubiquitin-proteasome system (UPS) and the autophagy-lysosome system (hereafter autophagy).

KEYWORDS:

autophagy-lysosome system; protein quality control; proteolysis; ubiquitin linkages; ubiquitination

PMID:
28947091
DOI:
10.1016/j.tibs.2017.09.002
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center