ArticleThe Journal of biological chemistry2008
Diacylglycerol specifically blocks spontaneous integration of membrane proteins and allows detection of a factor-assisted integration.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 48 citations in OpenAlex.
- Glycolipid MPIase, Essential for Membrane Protein Integration in the Cytoplasmic Membrane ofACS omega · 2026Article
- Article
- Membrane tubulation induced by a bacterial glycolipid.Scientific reports · 2025Article
- Article
- 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
- 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
- Eugene P. Kennedy's Legacy: Defining Bacterial Phospholipid Pathways and Function.Frontiers in molecular biosciences · 2021Review
- Article
- 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
- CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo.Scientific reports · 2019Article
- Cell-free synthesis of SecYEG translocon as the fundamental protein transport machinery.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2014Article
- Lipid dependencies, biogenesis and cytoplasmic micellar forms of integral membrane sugar transport proteins of the bacterial phosphotransferase system.Microbiology (Reading, England) · 2013Review
- Bacterial lipids: metabolism and membrane homeostasis.Progress in lipid research · 2013Review
- Article
- MPIase is a glycolipozyme essential for membrane protein integration.Nature communications · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We recently found that the spontaneous integration of M13 procoat is blocked by diacylglycerol (DAG) (Nishiyama, K., Ikegami, A., Moser, M., Schiltz, E., Tokuda, H., and Muller, M. (2006) J. Biol. Chem. 281, 35667-35676). Here, we demonstrate that the spontaneous integration of Pf3 coat, another membrane protein that has been thought to be integrated spontaneously into liposomes, can be blocked by DAG at physiological concentrations. Moreover, the spontaneous integration of the membrane potential-independent version of Pf3 coat (3L-Pf3 coat), which is independent of YidC, was also blocked by DAG. To clarify the mechanism by which DAG blocks spontaneous integration, we examined lipid compounds similar to DAG and DAG derivatives. The blockage of spontaneous integration was specific to DAG, as fatty acids, monoacylglycerol, and phosphatidic acids were not effective for the blockage. When the acyl chains in DAG were shortened even to octanoyl residues, it still blocked spontaneous integration, whereas diheptanoylglycerol did not block it at all. Triacylglycerol was more effective than DAG. However, the lipid A-derivative-dependent integration of M13 procoat could not be reconstituted when triacylglycerol was included in the liposomes. On the other hand, when DAG was included in the liposomes, we found that the integration of 3L-Pf3 coat was strictly dependent on the lipid A-derived integration factor. We propose that the bulky structure of DAG rather than changes in membrane curvature is essential for the blockage of spontaneous integration. We also demonstrated that the blockage of spontaneous integration by DAG is also operative in native membrane vesicles.
Indexed as
Identifiers
What OpenQuestion holds
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.