Results 31 to 40 of about 2,589 (171)

Protein lactylation in kidney diseases

open access: yesFrontiers in Cell and Developmental Biology
Post-translational modifications (PTMs) regulate protein function and structure through covalent modifications, participating in various physiological and pathological processes.
Yelei Xu   +4 more
doaj   +1 more source

Research progress and prospect of histone lactylation in digestive system tumors [PDF]

open access: yesZhongguo aizheng zazhi
Histone lactylation is a novel type of post-translational modification, where a lactate molecule covalently binds to the lysine residues of histones. This modification plays a key role in cellular metabolic reprogramming, particularly in digestive system
ZENG Dandan, LUO Wenfeng, YE Jiazhou, LIN Yan, LIANG Rong
doaj   +1 more source

Palmitoylation‐Mediated Ubiquitination of SRPK1 Regulates Ferroptosis in High‐Fat‐Induced Erectile Dysfunction

open access: yesAdvanced Science, EarlyView.
Elevated exogenous palmitic acid promotes the S‐palmitoylation of SRPK1 in endothelial cells, a dynamic process governed by ZDHHC24 and APT1. This post‐translational modification strengthens the interaction between SRPK1 and the E3 ubiquitin ligase MIB1, thereby facilitating the proteasomal degradation of SRPK1.
Xiao‐Hui Tan   +11 more
wiley   +1 more source

Protein Lactylation: A new jewel in the crown

open access: yesAsian Journal of Medical Sciences
Lactylation is a newly identified post-translational modification that has emerged as a crucial epigenetic regulator, significantly influencing cellular functions and disease processes. Lactylation involves the addition of lactate, a glycolysis byproduct,
Ruby Dhar   +2 more
doaj   +1 more source

Ufmylation‐Deficient DDRGK1 Ameliorates Obesity by Inhibiting FASN‐Mediated Adipocyte Lipogenesis

open access: yesAdvanced Science, EarlyView.
DDRGK1 regulates de novo lipogenesis via stabilization of fatty acid synthase (FASN). DDRGK1‐mediated UFMylation of FASN prevents its ubiquitin–proteasomal degradation. Reduced DDRGK1 expression or mutation at the key UFMylation site enhances FASN degradation and suppresses fatty acid synthesis (FAS), resulting in smaller adipocytes and improved ...
Yin Li   +16 more
wiley   +1 more source

UBE2T‐Driven p53 Degradation Rewires Glycolysis to Orchestrate Lactylation‐Mediated CAFs Activation and ECM Deposition in Pancreatic Cancer

open access: yesAdvanced Science, EarlyView.
This study integrates multi‐omics to reveal the critical role of UBE2T in driving malignancy and stromal co‐evolution in PDAC. UBE2T potentiates glycolysis by regulating p53 degradation via a positive feedback loop, thereby promoting histone H3 lysine 18 lactylation in CAFs and stromal deposition. The UBE2T inhibitor PGG represents a potential strategy
Yong Ma   +16 more
wiley   +1 more source

HAT1 functions as a lactyltransferase and mediates RPA1 lactylation to promote DNA repair and radioresistance in lung adenocarcinoma

open access: yesCell Death and Disease
Lysine lactylation is a post-translational modification induced by lactate discovered in recent years. Abnormal lysine lactylation contributes to the occurrence and progression of various tumors.
Jiang He   +16 more
doaj   +1 more source

Targeting Lactate and Lactylation in Cancer Metabolism and Immunotherapy

open access: yesAdvanced Science, EarlyView.
Lactate, once deemed a metabolic waste, emerges as a central regulator of cancer progression. This review elucidates how lactate and its epigenetic derivative, protein lactylation, orchestrate tumor metabolism, immune suppression, and therapeutic resistance.
Jiajing Gong   +5 more
wiley   +1 more source

Flipping the Switch: MeCP2‐Mediated Lactylation Rewires Microglial Metabolism and Inflammation via the HK2/mTOR Axis in Poststroke Neuroinflammation

open access: yesAdvanced Science
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

SLC2A3‐Mediated Lactate Metabolism Promotes Lung Cancer Bone Metastasis by Modulating P53 Lactylation and Immune Evasion

open access: yesAdvanced Science, EarlyView.
SLC2A3 derived lactate promotes metastasis through p53 lactylation at K120 and osteoclast differentiation. Pharmacological inhibition of SLC2A3 upregulates PD‐1 expression on CD8+ T cells via lactate induced p53 lactylation, which modulates immune evasion. ABSTRACT Bone metastasis is a devastating consequence of lung cancer.
Yi Ding   +10 more
wiley   +1 more source

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