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Histone lysine methylation modifiers controlled by protein stability

  • 작성자

    Jung-Ae Kim
  • 작성일자

    2024-12-26
  • 조회수

    379
Jung-Ae Kim ( jungaekim@kribb.re.kr )
2013-presentAssociate Professor, Department of Functional Genomics, UST KRIBB School, Daejeon, South KoreaAffiliation & Position
2012-presentPrincipal Investigator, KRIBB, Daejeon, South Korea
2008-2012Postdoctoral Associate, Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065, USA
2002-2008Ph.D. in Molecular and Cell Biology Program at Brandeis University, Waltham, MA 02453, USA
1999-2002Research Associate at National Creative Research Initiative Center for Cell Cycle Control, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, South Korea
1997-1999Master 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/