생화학분자생물학회입니다.
Histone lysine methylation modifiers controlled by protein stability
작성자
Jung-Ae Kim작성일자
2024-12-26조회수
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Jung-Ae Kim ( jungaekim@kribb.re.kr ) | |
2013-present | Associate Professor, Department of Functional Genomics, UST KRIBB School, Daejeon, South KoreaAffiliation & Position | |
2012-present | Principal Investigator, KRIBB, Daejeon, South Korea | |
2008-2012 | Postdoctoral Associate, Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065, USA | |
2002-2008 | Ph.D. in Molecular and Cell Biology Program at Brandeis University, Waltham, MA 02453, USA | |
1999-2002 | Research Associate at National Creative Research Initiative Center for Cell Cycle Control, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, South Korea | |
1997-1999 | Master of Science in Biochemistry at Korea University, Seoul, South Korea |
Histone lysine methylation modifiers controlled by protein stability
Histone lysine methylation is pivotal in shaping the epigenetic landscape and is linked to cell physiology. Coordination of the activities of multiple histone lysine methylation modifiers, namely, methyltransferases and demethylases, modulates chromatin structure and dynamically alters the epigenetic landscape, orchestrating almost all DNA-templated processes, such as transcription, DNA replication, and DNA repair. The stability of modifier proteins, which is regulated by protein degradation, is crucial for their activity. Here, we review the current knowledge of modifier-protein degradation via specific pathways and its subsequent impact on cell physiology through epigenetic changes. By summarizing the functional links between the aberrant stability of modifier proteins and human diseases and highlighting efforts to target protein stability for therapeutic purposes, we aim to promote interest in defining novel pathways that regulate the degradation of modifiers and ultimately increase the potential for the development of novel therapeutic strategies.
Exp Mol Med. 2024 Oct;56(10):2127-2144. doi: 10.1038/s12276-024-01329-5.
https://pubmed.ncbi.nlm.nih.gov/39394462/