ArticleJournal of the American Chemical Society2018
Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- An In Vitro Assay For LpxC Degradation By The Membrane-Bound Protease FtsH And Adaptor LapB From Escherichia coli.Journal of visualized experiments : JoVE · 2026Article
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Functional Nucleic Acid Probes Based on Two-Photon for Biosensing.Biosensors · 2023Review
- FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron.Molecular microbiology · 2023Article
- FtsH degrades dihydrofolate reductase by recognizing a partially folded species.Protein science : a publication of the Protein Society · 2022Article
- Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022Review
- Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reconstitution of Msp1 Extraction Activity with Fully Purified Components.Journal of visualized experiments : JoVE · 2021Article
- The AAA + ATPase valosin-containing protein (VCP)/p97/Cdc48 interaction network in Leishmania.Scientific reports · 2020Article
- Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease.The EMBO journal · 2020Article
- GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020Article
- Depletion of the FtsH1/3 Proteolytic Complex Suppresses the Nutrient Stress Response in the CyanobacteriumThe Plant cell · 2019Article
- Sorting out how Msp1 maintains mitochondrial membrane proteostasis.Mitochondrion · 2019Review
- On the Interpretation of Force-Induced Unfolding Studies of Membrane Proteins Using Fast Simulations.Biophysical journal · 2019Article
- Proteolysis mediated by the membrane-integrated ATP-dependent protease FtsH has a unique nonlinear dependence on ATP hydrolysis rates.Protein science : a publication of the Protein Society · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Energy landscape underlying spontaneous insertion and folding of an alpha-helical transmembrane protein into a bilayer.Nature communications · 2018Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
ATP-dependent protein degradation mediated by AAA+ proteases is one of the major cellular pathways for protein quality control and regulation of functional networks. While a majority of studies of protein degradation have focused on water-soluble proteins, it is not well understood how membrane proteins with abnormal conformation are selectively degraded. The knowledge gap stems from the lack of an in vitro system in which detailed molecular mechanisms can be studied as well as difficulties in studying membrane protein folding in lipid bilayers. To quantitatively define the folding-degradation relationship of membrane proteins, we reconstituted the degradation using the conserved membrane-integrated AAA+ protease FtsH as a model degradation machine and the stable helical-bundle membrane protein GlpG as a model substrate in the lipid bilayer environment. We demonstrate that FtsH possesses a substantial ability to actively unfold GlpG, and the degradation significantly depends on the stability and hydrophobicity near the degradation marker. We find that FtsH hydrolyzes 380-550 ATP molecules to degrade one copy of GlpG. Remarkably, FtsH overcomes the dual-energetic burden of substrate unfolding and membrane dislocation with the ATP cost comparable to that for water-soluble substrates by robust ClpAP/XP proteases. The physical principles elucidated in this study provide general insights into membrane protein degradation mediated by ATP-dependent proteolytic systems.
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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.