ArticleProceedings of the National Academy of Sciences of the United States of America2025
Higher-order transient membrane protein structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Article
- Article
- Spontaneous and indefinite blinking in upconverting nanoparticles for ångström-precision multicolour super-resolution imaging.Nature nanotechnology · 2026Article
- Spatial Deconstruction of the Plasma Membrane.Journal of the American Chemical Society · 2026Article
- Characterising C-X-C Chemokine Receptor 4 Dynamics in the Cell Membrane Using Fluorescence Fluctuation Spectroscopy.Biomolecules · 2026Article
- Membrane Models and the Pursuit of Coherence.Biochemistry · 2026Review
- Biomolecular assemblies through weak noncovalent interactions: Higher-order transient structures and their condensate phase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cholesterol, PtdIns(4,5)PbioRxiv : the preprint server for biology · 2026Article
- Unstructured transcription factor interactions enable emergent specificity.Science (New York, N.Y.) · 2026Article
- Affinity-guided labeling reveals P2X7 nanoscale membrane redistribution during BV2 microglial activation.eLife · 2026Article
- Cryogenic light microscopy of vitrified samples with angstrom precision.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A biased allosteric modulator functions as a molecular glue to induce βResearch square · 2025Article
- The configurational length scale in the self-assembly and modulation of higher-order transient protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.Nature communications · 2025Article
- A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025Article
- Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.bioRxiv : the preprint server for biology · 2025Article
- Detergent-free isolation and characterization of amyloid precursor protein C99 in E. coli native lipid-nanodiscs using non-ionic polymer.Protein science : a publication of the Protein Society · 2025Article
- Cryo-light microscopy with angstrom precision deciphers structural conformations of PIEZO1 in its native state.Science advances · 2025Article
- Molecular contacts in self-assembling clusters of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lipidic folding pathway of α-Synuclein via a toxic oligomer.Nature communications · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
This study shows that five membrane proteins-three GPCRs, an ion channel, and an enzyme-form self-clusters under natural expression levels in a cardiac-derived cell line. The cluster size distributions imply that these proteins self-oligomerize reversibly through weak interactions. When the concentration of the proteins is increased through heterologous expression, the cluster size distributions approach a critical distribution at which point a phase transition occurs, yielding larger bulk phase clusters. A thermodynamic model like that explaining micellization of amphiphiles and lipid membrane formation accounts for this behavior. We propose that many membrane proteins exist as oligomers that form through weak interactions, which we call higher-order transient structures (HOTS). The key characteristics of HOTS are transience, molecular specificity, and a monotonically decreasing size distribution that may become critical at high concentrations. Because molecular specificity invokes self-recognition through protein sequence and structure, we propose that HOTS are genetically encoded supramolecular units.
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