Abstract 2434 Autoregulatory mechanism of enzyme activity by the nuclear localization signal of lysine-specific demethylase 1
Lysine-specific histone demethylase 1 (LSD1) modulates transcription through the removal of methyl groups from lysine residues on histone 3 (H3K4Me1/2 or H3K9Me1/2), serving dual roles as a repressor or activator in gene regulation. Integral to its function, the N-terminal region of LSD1, characterized by an absence of structured elements, features a nuclear localization signal (NLS) that spans residues 112 to 117 (RRARAK). This region is rich in post-translational modifications and serves as a crucial node for protein interactions.
Authors
- Zigmund Luka (ORCID: https://orcid.org/0000-0003-4079-7459)
- Alexander Hirschi
- Roshni Patel (ORCID: https://orcid.org/0000-0002-1399-3131)
- Dulmi Senanayaka
- Nicholas Reiter
- Sahar Alishiri
- William Martin (ORCID: https://orcid.org/0000-0003-4839-1752)
- Danyun Zeng
- Khadijah I. Moore
Institutions
- Marquette University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109293
- Primary Topic
- Epigenetics and DNA Methylation
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation