ArticleBiophysical journal2009
Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 105 citations in OpenAlex.
- Binding orientation of weakly associating membrane peripheral proteins via membrane paramagnetic relaxation enhancement NMR.Communications chemistry · 2026Article
- Review
- Cooperativity of PIP2 and PS lipids modulates PH domain binding.Biophysical journal · 2025Article
- PDK1:PKCα heterodimer association-dissociation dynamics in single-molecule diffusion tracks on a target membrane.Biophysical journal · 2023Article
- Stimulation of the catalytic activity of the tyrosine kinase Btk by the adaptor protein Grb2.eLife · 2023Article
- Maximum likelihood-based estimation of diffusion coefficient is quick and reliable method for analyzing estradiol actions on surface receptor movements.Frontiers in neuroinformatics · 2023Article
- Systematic simulation of the interactions of pleckstrin homology domains with membranes.Science advances · 2022Article
- Curvature dependence of BAR protein membrane association and dissociation kinetics.Scientific reports · 2022Article
- Single-molecule studies reveal regulatory interactions between master kinases PDK1, AKT1, and PKC.Biophysical journal · 2021Article
- A short C-terminal peptide in Gγ regulates Gβγ signaling efficacy.Molecular biology of the cell · 2021Article
- Molecular motion and tridimensional nanoscale localization of kindlin control integrin activation in focal adhesions.Nature communications · 2021Article
- The G-Protein Rab5A Activates VPS34 Complex II, a Class III PI3K, by a Dual Regulatory Mechanism.Biophysical journal · 2020Article
- Cadherin clusters stabilized by a combination of specific and nonspecific cis-interactions.eLife · 2020Article
- Single-molecule imaging of PI(4,5)PCommunications biology · 2020Article
- Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes.Science advances · 2020Article
- Article
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- PI(4,5)P2 determines the threshold of mechanical force-induced B cell activation.The Journal of cell biology · 2018Article
- Single-Molecule Study Reveals How Receptor and Ras Synergistically Activate PI3Kα and PIPBiophysical journal · 2017Article
- Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteins containing membrane targeting domains play essential roles in many cellular signaling pathways. However, important features of the membrane-bound state are invisible to bulk methods, thereby hindering mechanistic analysis of membrane targeting reactions. Here we use total internal reflection fluorescence microscopy (TIRFM), combined with single particle tracking, to probe the membrane docking mechanism of a representative pleckstrin homology (PH) domain isolated from the general receptor for phosphoinositides, isoform 1 (GRP1). The findings show three previously undescribed features of GRP1 PH domain docking to membranes containing its rare target lipid, phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P(3)]. First, analysis of surface diffusion kinetics on supported lipid bilayers shows that in the absence of other anionic lipids, the PI(3,4,5)P(3)-bound protein exhibits the same diffusion constant as a single lipid molecule. Second, the binding of the anionic lipid phosphatidylserine to a previously unidentified secondary binding site slows both diffusion and dissociation kinetics. Third, TIRFM enables direct observation of rare events in which dissociation from the membrane surface is followed by transient diffusion through solution and rapid rebinding to a nearby, membrane-associated target lipid. Overall, this study shows that in vitro single-molecule TIRFM provides a new window into the molecular mechanisms of membrane docking reactions.
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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.