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Updated: Apr 9, 2026
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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
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Protein monoubiquitylation: targets and diverse functions
Tadashi Nakagawa1, Keiko Nakayama1
1Division of Cell Proliferation, ART, Graduate School of Medicine, Tohoku University, Sendai, 980-8575, Miyagi, Japan.
Summary
Protein ubiquitylation, a post-translational modification, involves attaching ubiquitin to targets. This summary focuses on protein monoubiquitylation, exploring its targets and functions, which are increasingly recognized as biologically important.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Ubiquitin is a 76-amino acid protein involved in post-translational modification.
- Protein ubiquitylation involves the covalent attachment of ubiquitin to substrate proteins, typically at internal lysine residues.
- Polyubiquitylation forms ubiquitin chains, with distinct linkages (e.g., Lys-63, Met-1) mediating different cellular functions like DNA repair or proteasomal degradation.
Purpose of the Study:
- To summarize recent findings on protein monoubiquitylation.
- To provide an overview of the targets of protein monoubiquitylation.
- To elucidate the molecular functions of protein monoubiquitylation.
Main Methods:
- Review of recent proteomics analyses.
- Synthesis of current research on protein monoubiquitylation.
- Analysis of identified substrate targets and their associated functions.
Main Results:
- Protein monoubiquitylation occurs more frequently than polyubiquitylation.
- While functions of monoubiquitylation were previously unclear, recent studies reveal its biological significance.
- Specific targets and molecular roles of monoubiquitylation are beginning to be identified.
Conclusions:
- Protein monoubiquitylation is a prevalent and functionally important post-translational modification.
- Further research is crucial for a comprehensive understanding of monoubiquitylation's diverse roles.
- This modification plays a key role in various cellular processes beyond protein degradation.
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