ArticleBiophysical journal2006
Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Quantifying Small-Molecule Association with Lipid Membranes: Methods, Models, and Limitations.Membranes · 2026Review
- Charge-based immunoreceptor signalling in health and disease.Nature reviews. Immunology · 2025Review
- Cooperativity of PIP2 and PS lipids modulates PH domain binding.Biophysical journal · 2025Article
- PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022Article
- Review
- Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function.Membranes · 2021Review
- PIPProceedings of the National Academy of Sciences of the United States of America · 2020Review
- The Bilayer Collective Properties Govern the Interaction of an HIV-1 Antibody with the Viral Membrane.Biophysical journal · 2020Article
- Effects of Membrane Charge and Order on Membrane Binding of the Retroviral Structural Protein Gag.Journal of virology · 2016Article
- Article
- The emerging role of phosphoinositide clustering in intracellular trafficking and signal transduction.F1000Research · 2016Review
- Helix 8 of the angiotensin- II type 1A receptor interacts with phosphatidylinositol phosphates and modulates membrane insertion.Scientific reports · 2015Article
- Nanodomains in early and later phases of FcɛRI signalling.Essays in biochemistry · 2015Article
- Article
- Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction.Biology open · 2014Article
- Effect of polyelectrolyte adsorption on lateral distribution and dynamics of anionic lipids: a Monte Carlo study of a coarse-grain model.European biophysics journal : EBJ · 2014Article
- Counterion-mediated cluster formation by polyphosphoinositides.Chemistry and physics of lipids · 2014Review
- Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3.Biochemistry · 2014Article
- Compositional redistribution and dynamic heterogeneity in mixed lipid membrane induced by polyelectrolyte adsorption: effects of chain rigidity.The European physical journal. E, Soft matter · 2014Article
- Defining the oligomerization state of γ-synuclein in solution and in cells.Biochemistry · 2014Article
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Authors and funding
6 authors.
Funding
Abstract
Several biologically important peripheral (e.g., myristoylated alanine-rich C kinase substrate) and integral (e.g., the epidermal growth factor receptor) membrane proteins contain clusters of basic residues that interact with acidic lipids in the plasma membrane. Previous measurements demonstrate that the polyvalent acidic lipid phosphatidylinositol 4,5-bisphosphate is bound electrostatically (i.e., sequestered) by membrane-adsorbed basic peptides corresponding to these clusters. We report here three experimental observations that suggest monovalent acidic lipids are not sequestered by membrane-bound basic peptides. 1), Binding of basic peptides to vesicles does not decrease when the temperature is lowered below the fluid-to-gel phase transition. 2), The binding energy of Lys-13 to lipid vesicles increases linearly with the fraction of monovalent acidic lipids. 3), Binding of basic peptides to vesicles produces no self-quenching of fluorescent monovalent acidic lipids. One potential explanation for these results is that membrane-bound basic peptides diffuse too rapidly for the monovalent lipids to be sequestered. Indeed, our fluorescence correlation spectroscopy measurements show basic peptides bound to phosphatidylcholine/phosphatidylserine membranes have a diffusion coefficient approximately twofold higher than that of lipids, and those bound to phosphatidylcholine/phosphatidylinositol 4,5-bisphosphate membranes have a diffusion coefficient comparable to that of lipids.
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