ArticleBiophysical journal2019
Alteration of Membrane Physicochemical Properties by Two Factors for Membrane Protein Integration.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Glycolipid MPIase, Essential for Membrane Protein Integration in the Cytoplasmic Membrane ofACS omega · 2026Article
- Membrane tubulation induced by a bacterial glycolipid.Scientific reports · 2025Article
- Review
- Structures, functions, and syntheses of glycero-glycophospholipids.Frontiers in chemistry · 2024Review
- Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Role of a bacterial glycolipid in Sec-independent membrane protein insertion.Scientific reports · 2022Article
- Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane ofFrontiers in molecular biosciences · 2022Review
- The bacterial protein YidC accelerates MPIase-dependent integration of membrane proteins.The Journal of biological chemistry · 2019Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
After a nascent chain of a membrane protein emerges from the ribosomal tunnel, the protein is integrated into the cell membrane. This process is controlled by a series of proteinaceous molecular devices, such as signal recognition particles and Sec translocons. In addition to these proteins, we discovered two endogenous components regulating membrane protein integration in the inner membrane of Escherichia coli. The integration is blocked by diacylglycerol (DAG), whereas the blocking is relieved by a glycolipid named membrane protein integrase (MPIase). Here, we investigated the influence of these integration-blocking and integration-promoting factors on the physicochemical properties of membrane lipids via solid-state NMR and fluorescence measurements. These factors did not have destructive effects on membrane morphology because the membrane maintained its lamellar structure and did not fuse in the presence of DAG and/or MPIase at their effective concentrations. We next focused on membrane flexibility. DAG did not affect the mobility of the membrane surface, whereas the sugar chain in MPIase was highly mobile and enhanced the flexibility of membrane lipid headgroups. Comparison with a synthetic MPIase analog revealed the effects of the long sugar chain on membrane properties. The acyl chain order inside the membrane was increased by DAG, whereas the increase was cancelled by the addition of MPIase. MPIase also loosened the membrane lipid packing. Focusing on the transbilayer movement, MPIase reduced the rapid flip-flop motion of DAG. On the other hand, MPIase could not compensate for the diminished lateral diffusion by DAG. These results suggest that by manipulating the membrane lipids dynamics, DAG inhibits the protein from contacting the inner membrane, whereas the flexible long sugar chain of MPIase increases the opportunity for interaction between the membrane and the protein, leading to membrane integration of the newly formed protein.
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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.