Nonhistone Lysine Methylation as a Protein Degradation Signal
Protein degradation is a fundamental feature of cellular life, and malfunction of this process is implicated in human disease. Ubiquitin tagging is the best characterized mechanism of targeting a protein for degradation; however, there are a growing number of distinct mechanisms which have also been...
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Wiley
2022-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2022/1969299 |
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| author | Nicholas A. Lehning Brad E. Morrison |
| author_facet | Nicholas A. Lehning Brad E. Morrison |
| author_sort | Nicholas A. Lehning |
| collection | DOAJ |
| description | Protein degradation is a fundamental feature of cellular life, and malfunction of this process is implicated in human disease. Ubiquitin tagging is the best characterized mechanism of targeting a protein for degradation; however, there are a growing number of distinct mechanisms which have also been identified that carry out this essential function. For example, covalent tagging of proteins with sequestosome-1 targets them for selective autophagy. Degradation signals are not exclusively polypeptides such as ubiquitin, NEDD8, and sequestosome-1. Phosphorylation, acetylation, and methylation are small covalent additions that can also direct protein degradation. The diversity of substrate sequences and overlap with other pleotrophic functions for these smaller signaling moieties has made their characterization more challenging. However, these small signals might be responsible for orchestrating a large portion of the protein degradation activity in the cell. As such, there has been increasing interest in lysine methylation and associated lysine methyltransferases (KMTs), beyond canonical histone protein modification, in mediating protein degradation in a variety of contexts. This review focuses on the current evidence for lysine methylation as a protein degradation signal with a detailed discussion of the class of enzymes responsible for this phenomenon. |
| format | Article |
| id | doaj-art-5e99643ae3dc4af0b50ff496fd29b22e |
| institution | Kabale University |
| issn | 2090-9071 |
| language | English |
| publishDate | 2022-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Chemistry |
| spelling | doaj-art-5e99643ae3dc4af0b50ff496fd29b22e2025-08-20T03:34:33ZengWileyJournal of Chemistry2090-90712022-01-01202210.1155/2022/1969299Nonhistone Lysine Methylation as a Protein Degradation SignalNicholas A. Lehning0Brad E. Morrison1Biomolecular Ph.D. ProgramBiomolecular Ph.D. ProgramProtein degradation is a fundamental feature of cellular life, and malfunction of this process is implicated in human disease. Ubiquitin tagging is the best characterized mechanism of targeting a protein for degradation; however, there are a growing number of distinct mechanisms which have also been identified that carry out this essential function. For example, covalent tagging of proteins with sequestosome-1 targets them for selective autophagy. Degradation signals are not exclusively polypeptides such as ubiquitin, NEDD8, and sequestosome-1. Phosphorylation, acetylation, and methylation are small covalent additions that can also direct protein degradation. The diversity of substrate sequences and overlap with other pleotrophic functions for these smaller signaling moieties has made their characterization more challenging. However, these small signals might be responsible for orchestrating a large portion of the protein degradation activity in the cell. As such, there has been increasing interest in lysine methylation and associated lysine methyltransferases (KMTs), beyond canonical histone protein modification, in mediating protein degradation in a variety of contexts. This review focuses on the current evidence for lysine methylation as a protein degradation signal with a detailed discussion of the class of enzymes responsible for this phenomenon.http://dx.doi.org/10.1155/2022/1969299 |
| spellingShingle | Nicholas A. Lehning Brad E. Morrison Nonhistone Lysine Methylation as a Protein Degradation Signal Journal of Chemistry |
| title | Nonhistone Lysine Methylation as a Protein Degradation Signal |
| title_full | Nonhistone Lysine Methylation as a Protein Degradation Signal |
| title_fullStr | Nonhistone Lysine Methylation as a Protein Degradation Signal |
| title_full_unstemmed | Nonhistone Lysine Methylation as a Protein Degradation Signal |
| title_short | Nonhistone Lysine Methylation as a Protein Degradation Signal |
| title_sort | nonhistone lysine methylation as a protein degradation signal |
| url | http://dx.doi.org/10.1155/2022/1969299 |
| work_keys_str_mv | AT nicholasalehning nonhistonelysinemethylationasaproteindegradationsignal AT brademorrison nonhistonelysinemethylationasaproteindegradationsignal |