ArticleNature communications2012
MPIase is a glycolipozyme essential for membrane protein integration.
Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 59 citations in OpenAlex.
- Dark Side ofJournal of the American Chemical Society · 2026Article
- Glycolipid MPIase, Essential for Membrane Protein Integration in the Cytoplasmic Membrane ofACS omega · 2026Article
- The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025Review
- Membrane tubulation induced by a bacterial glycolipid.Scientific reports · 2025Article
- CdsA, a CDP-diacylglycerol synthase involved in phospholipid and glycolipid MPIase biosynthesis, possesses multiple initiation codons.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- Review
- Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Structures, functions, and syntheses of glycero-glycophospholipids.Frontiers in chemistry · 2024Review
- Phosphatidylglycerol Is the Lipid Donor for Synthesis of Phospholipid-Linked Enterobacterial Common Antigen.Journal of bacteriology · 2023Article
- Role of a bacterial glycolipid in Sec-independent membrane protein insertion.Scientific reports · 2022Article
- Interplay between MPIase, YidC, and PMF during Sec-independent insertion of membrane proteins.Life science alliance · 2022Article
- Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane ofFrontiers in molecular biosciences · 2022Review
- A Relationship between NTP and Cell Extract Concentration for Cell-Free Protein Expression.Life (Basel, Switzerland) · 2021Article
- Article
- CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis.Frontiers in cell and developmental biology · 2020Review
- The bacterial protein YidC accelerates MPIase-dependent integration of membrane proteins.The Journal of biological chemistry · 2019Article
- Alteration of Membrane Physicochemical Properties by Two Factors for Membrane Protein Integration.Biophysical journal · 2019Article
- Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography.The protein journal · 2019Review
- Increased expression of the bacterial glycolipid MPIase is required for efficient protein translocation across membranes in cold conditions.The Journal of biological chemistry · 2019Article
- CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein integration into biological membranes is a vital cellular event for all organisms. We previously reported an integration factor in the inner membrane of Escherichia coli, named MPIase (membrane protein integrase). Here we show that in contrast to previously identified integration factors that are proteins, MPIase is a glycolipid composed of diacylglycerol and a glycan chain of three acetylated aminosugars linked through pyrophosphate. Hydrolytic removal of the lipid moiety gives a soluble product with higher integration activity than that of the original MPIase. This soluble form of MPIase directly interacts with a newborn membrane protein, maintaining its integration-competent structure and allowing its post-translational integration. MPIase actively drives protein integration following chaperoning membrane proteins. We further demonstrate with anti-MPIase antibodies that MPIase is likely involved in integration in vivo. Collectively, our results suggest that MPIase, essential for membrane protein integration, is to our knowledge the first glycolipid with an enzyme-like activity.
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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.