ArticleNature communications2022
Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
45 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- LpxC activity regulation: An emerging paradigm for controlling lipopolysaccharide synthesis.Trends in microbiology · 2026Article
- Adhesion-Enhanced Engineered Probiotic for Prolonged Intestinal Retention and Calprotectin-Responsive IBD Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Protein-Protein Interactions Between Peptidoglycan, Lipopolysaccharide, and Phospholipid Biosynthesis Enzymes in Escherichia coli.Chembiochem : a European journal of chemical biology · 2026Article
- Loss of O-antigen due toScience advances · 2026Article
- Control of the committed step in lipopolysaccharide biosynthesis.The Journal of biological chemistry · 2026Review
- Article
- Structural Evolution and Immunomodulatory Versatility of Fungal Immunomodulatory Proteins: Insights into Mechanisms and Bioproduction Strategies.Journal of agricultural and food chemistry · 2026Review
- Integrated Fermentation Engineering Enables High-Level Leghemoglobin Production in Kluyveromyces marxianus via Metabolic Rewiring of Central Carbon Metabolism and Amino Acid Utilization.Biotechnology journal · 2026Article
- PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae.Nucleic acids research · 2026Article
- A potential role for acyl-phosphate in the coordination of phospholipid and lipopolysaccharide synthesis inbioRxiv : the preprint server for biology · 2026Article
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- Therapeutic milestones against multidrug resistant Acinetobacter baumannii: from legacy antibiotics to Zosurabalpin.Archives of microbiology · 2026Review
- Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026Article
- Membrane perturbation by the last-resort antibiotic polymyxin B drives biphasic regulation of horizontal gene transfer.The ISME journal · 2026Article
- Eco-friendly dyeing of silk fabric by usingRSC advances · 2025Article
- Virulence arresting drug discovery by strategies targeting bacterial virulence: Mainly focusing on quorum-sensing interference and biofilm inhibition.Journal of pharmaceutical analysis · 2025Review
- Coordinated Biosynthesis of Essential Cell Envelope Components: Lipopolysaccharide and Fatty Acids Requires LapD, Acyl Carrier Protein, and Fully Hexaacylated Lipid A.International journal of molecular sciences · 2025Article
- Causal Relationship Between Gut Microbiota and Benign Prostatic Hyperplasia: A Two-Sample Mendelian Randomization Analyses, 16S rRNA Sequencing and Clinical Retrospective Study.Food science & nutrition · 2025Article
- AcuteMicroorganisms · 2025Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Lipopolysaccharide (LPS) is an essential glycolipid and forms a protective permeability barrier for most Gram-negative bacteria. In E. coli, LPS levels are under feedback control, achieved by FtsH-mediated degradation of LpxC, which catalyzes the first committed step in LPS synthesis. FtsH is a membrane-bound AAA+ protease, and its protease activity toward LpxC is regulated by essential membrane proteins LapB and YejM. However, the regulatory mechanisms are elusive. We establish an in vitro assay to analyze the kinetics of LpxC degradation and demonstrate that LapB is an adaptor protein that utilizes its transmembrane helix to interact with FtsH and its cytoplasmic domains to recruit LpxC. Our YejM/LapB complex structure reveals that YejM is an anti-adaptor protein, competing with FtsH for LapB to inhibit LpxC degradation. Structural analysis unravels that LapB and LPS have overlapping binding sites in YejM. Thus, LPS levels control formation of the YejM/LapB complex to determine LpxC protein levels.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.