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Related Concept Videos

GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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Related Experiment Video

Updated: Jun 23, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Lactylation: a novel post-translational modification for cGAS-STING pathway.

Hongquan Wang1,2,3, Zhiji Wang4, Fanyu Meng5

  • 1Department of Geriatrics, Aerospace Center Hospital, Peking University Aerospace School of Clinical Medicine, Beijing, 100049, China.

Inflammation Research : Official Journal of the European Histamine Research Society ... [Et Al.]
|June 20, 2026
PubMed
Summary
This summary is machine-generated.

Lysine lactylation (Kla) regulates the cGAS-STING pathway, impacting innate immunity in various diseases. Targeting this metabolic-epigenetic modification offers novel therapeutic strategies for autoimmune disorders, cancer, and neuroinflammation.

Keywords:
LactylationPost-translational modificationSTINGcGAS

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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

Related Experiment Videos

Last Updated: Jun 23, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

Area of Science:

  • Immunometabolism
  • Epigenetics
  • Post-translational modifications

Background:

  • Lysine lactylation (Kla) is a metabolic-epigenetic regulator linking cellular metabolism to innate immune signaling.
  • The cGAS-STING pathway is crucial for innate immunity and is influenced by metabolic states.
  • The specific role of lactylation in modulating the cGAS-STING pathway requires synthesis.

Purpose of the Study:

  • To analyze the molecular mechanisms of lysine lactylation in regulating the cGAS-STING signaling axis.
  • To discuss the pathophysiological implications of lactylation in diseases.
  • To explore the therapeutic potential of targeting lactylation in autoimmunity, neuroinflammation, and cancer.

Main Methods:

  • Comprehensive literature review.
  • Summarized the biochemical basis of lactylation (writers, erasers, readers).
  • Examined evidence of direct and indirect regulation of cGAS-STING by lactylation, including disease models and therapeutic interventions.

Main Results:

  • Lactylation directly modifies cGAS and STING, affecting their stability, activity, and signaling.
  • Lactylation has dual effects: enhancing interferon responses in autoimmune diseases and hypoxic-ischemic encephalopathy, but suppressing cGAS-STING in cancer and neuropathic pain.
  • Indirect regulation involves lactylation's influence on cytosolic DNA availability and repair, with identified lactyltransferases and delactylases.

Conclusions:

  • Lactylation acts as a metabolic-immune checkpoint, fine-tuning cGAS-STING signaling in a disease-specific manner.
  • Targeting the lactylation axis presents a novel immunometabolic therapeutic strategy.
  • Potential applications include treating autoimmune disorders, chronic infections, neurodegeneration, and cancer.