ArticleBiochimica et biophysica acta2008
Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding.
Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Robust and resource-optimal dynamic pattern formation of Min proteins in vivo.Nature physics · 2025Article
- The E. coli MinCDE system in the regulation of protein patterns and gradients.Cellular and molecular life sciences : CMLS · 2019Review
- MadR1, a Mycobacterium tuberculosis cell cycle stress response protein that is a member of a widely conserved protein class of prokaryotic, eukaryotic and archeal origin.Tuberculosis (Edinburgh, Scotland) · 2015Article
- The membrane: transertion as an organizing principle in membrane heterogeneity.Frontiers in microbiology · 2015Review
- A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function.Biochimica et biophysica acta · 2013Review
- MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli.The Journal of biological chemistry · 2012Article
- Advances in understanding E. coli cell fission.Current opinion in microbiology · 2010Review
- Membrane potential is important for bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cardiolipin membrane domains in prokaryotes and eukaryotes.Biochimica et biophysica acta · 2009Review
- Molecular genetic approaches to defining lipid function.Journal of lipid research · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
MinD, a well-conserved bacterial amphitropic protein involved in spatial regulation of cell division, has a typical feature of reversible binding to the membrane. MinD shows a clear preference for acidic phospholipids organized into lipid domains in bacterial membrane. We have shown that binding of MinD may change the dynamics of model and native membranes (see accompanying paper [1]). On the other hand, MinD dimerization and anchoring could be enhanced on pre-existing anionic phospholipid domains. We have tested MinD binding to model membranes in which acidic and zwitterionic phospholipids are either well-mixed or segregated to phase domains. The phase separation was achieved in binary mixtures of 1-Stearoyl-2-Oleoyl-sn-Glycero-3-[Phospho-rac-(1-glycerol] (SOPG) with 1,2-Distearoyl-sn-Glycero-3-Phosphocholine (DSPC) or 1,2-Distearoyl-sn-Glycero-3-[Phospho-rac-(1-glycerol)] (DSPG) and binding to these membranes was compared with that to a fluid mixture of SOPG with 1-Stearoyl-2-Oleoyl-sn-Glycero-3-Phosphocholine (SOPC). The results demonstrate that MinD binding to the membrane is enhanced by segregation of anionic phospholipids to fluid domains in a gel-phase environment and, moreover, the protein stabilizes such domains. This suggests that an uneven binding of MinD to the heterogeneous native membrane is possible, leading to formation of a lipid-specific distribution pattern of MinD and/or modulation of its temporal behavior.
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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.