Xuejun Jiang

Mar 20, 2024 | nature.com | Zhiming Li |Zhiguo Zhang |Xuejun Jiang |Brent R. Stockwell

AbstractYEATS domain-containing protein GAS41 is a histone reader and oncogene. Here, through genome-wide CRISPR-Cas9 screenings, we identify GAS41 as a repressor of ferroptosis. GAS41 interacts with NRF2 and is critical for NRF2 to activate its targets such as SLC7A11 for modulating ferroptosis. By recognizing the H3K27-acetylation (H3K27-ac) marker, GAS41 is recruited to the SLC7A11 promoter, independent of NRF2 binding.

Feb 29, 2024 | nature.com | Enyong Dai |Xin McRae Chen |Xuejun Jiang |Rui Kang |Valerian E. Kagan |Ana J. García-Sáez | +27 more

AbstractFerroptosis, an intricately regulated form of cell death characterized by uncontrolled lipid peroxidation, has garnered substantial interest since this term was first coined in 2012. Recent years have witnessed remarkable progress in elucidating the detailed molecular mechanisms that govern ferroptosis induction and defence, with particular emphasis on the roles of heterogeneity and plasticity.

Oct 31, 2023 | nature.com | Zheng Fan |Matthew Miele |Xuejun Jiang

Correction to: Nature https://doi.org/10.1038/s41586-023-05780-8 Published online 1 March 2023In the originally published version of the paper, the bottom photo in Extended Data Figure 8d was a duplicate of the second photo. We have corrected this inadvertent mistake in the HTML and PDF versions of the article. Additionally, to improve readability, we have updated Supplementary Figure 4 to now spread over three pages.

Mar 20, 2023 | nature.com | Zheng Fan |Matthew Miele |Xuejun Jiang

Correction to: Nature https://doi.org/10.1038/s41586-023-05780-8 Published online 1 March 2023In the version of this article initially published, the range of units shown along the x-axis label of the third panel in Fig. 2e was incorrect, and has been updated to read “2 h, 4 h, 8 h, 24 h, 48 h” from the original “2 h, 8 h, 24 h, 8 h, 48 h”. The errors have been corrected in the HTML and PDF versions of the article.

Mar 1, 2023 | nature.com | Zheng Fan |Matthew Miele |Xuejun Jiang

AbstractTrimethylation of histone H3 lysine 4 (H3K4me3) is associated with transcriptional start sites and has been proposed to regulate transcription initiation1,2. However, redundant functions of the H3K4 SET1/COMPASS methyltransferase complexes complicate the elucidation of the specific role of H3K4me3 in transcriptional regulation3,4.