Results 51 to 60 of about 119,118 (204)
Tian et al. reveal that FH K112 lactylation is elevated after TBI, leading to fumarate accumulation, mitochondrial damage, mtDNA release and amplified neuroinflammation. AARS2 and SIRT3 act as the “writer” and “eraser” for FH K112 lactylation. The peptide Pep‐K112 targeting this site alleviates brain injury, highlighting a potential therapeutic target.
Yang Tian +21 more
wiley +1 more source
Microglial metabolic/inflammatory reprogramming critically influences stroke outcomes, yet its mechanisms remain poorly understood. Lysine lactylation, an epigenetic modification in which lactate‐derived lactyl groups modify lysine residues, regulates ...
Zengyu Zhang +12 more
doaj +1 more source
Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea. [PDF]
Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification in Botrytis cinerea, a destructive necrotrophic fungal ...
Gao M, Zhang N, Liang W.
europepmc +5 more sources
The SIRT5/ACAA2 axis maintains lipid metabolic homeostasis in RTECs by promoting ACAA2 desuccinylation and preserving its stability and enzymatic activity, thereby sustaining FAO and limiting PUFA and PUFA‐containing phospholipid accumulation. Under CaOx stress, SIRT5 downregulation impairs FAO, promotes oxidative stress and ferroptosis, and enhances ...
Qinhong Jiang +6 more
wiley +1 more source
Hypoxia, abnormal perfusion, and oncogenic signaling increase lactate production in lung cancer and create intercellular fluxes mediated by monocarboxylate transporters. Circulating lactate can be taken up by lung tumors and enter the tricarboxylic acid (
Zihao Lin, Chengri Che, Shuwei Wang
doaj +1 more source
Non-histone lactylation: unveiling its functional significance [PDF]
Lactylation, a newly discovered protein posttranslational modification (PTM) in 2019, primarily occurs on lysine residues. Lactylation of histones was initially identified, and subsequent studies have increasingly demonstrated its widespread presence on ...
Shaolu Zhang, Yongjie Ma, Pusong Shi
core +1 more source
Lactate‐driven endometrial cancer relapse is mediated by enzymatic protein modification. Elevated lactate levels activate AARS1, which catalyzes K280 lactylation of IGF2BP3, therefore stabilizing HMGA2 mRNA and promoting tumor stemness and recurrence.
Peng Jiang +11 more
wiley +1 more source
A glycolysis‐driven epigenetic switch promotes therapy resistance in meningioma. Increased lactate production enhances histone H3K27 lactylation, which activates PROS1 secretion. Secreted PROS1 engages TYRO3 signaling to degrade the senescence regulator CARF, allowing cancer cells to escape growth arrest.
Zhuohang Wang +12 more
wiley +1 more source
Background Early embryo loss is an important factor affecting the reproductive capacity of cattle. Recent studies have revealed that during the process of embryonic genome activation (EGA), epigenetic modification, such as histone lactylation remodeling,
Wenjie Yu +10 more
doaj +1 more source
Aspirin‐Derived Salicyl‐CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2
Aspirin‐derived salicyl‐CoA serves as a previously unrecognized acyl donor for protein lysine salicylation. This study identifies histone lysine salicylation as a reversible epigenetic modification regulated by CBP and SIRT2, expanding the biochemical actions of aspirin beyond its canonical acetylation‐dependent mechanisms and providing a new framework
Facai Zhang +15 more
wiley +1 more source

