ArticleThe Journal of chemical physics2021
Speed limits of protein assembly with reversible membrane localization.
Article in The Journal of chemical physics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026Article
- Mechanisms of enhanced or impaired DNA target selectivity driven by protein dimerization.PNAS nexus · 2026Article
- Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell.The journal of physical chemistry. B · 2026Article
- A membrane-driven biochemical oscillator tunable by the volume to surface area ratio.bioRxiv : the preprint server for biology · 2025Article
- An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.Nature communications · 2025Article
- Mechanisms of enhanced or impaired DNA target selectivity driven by protein dimerization.bioRxiv : the preprint server for biology · 2025Article
- Enzymatic Reactions Dictated by the 2D Membrane Environment.The journal of physical chemistry letters · 2025Article
- Conformational dynamics and membrane insertion mechanism of B4GALNT1 in ganglioside synthesis.Nature communications · 2025Article
- Parallelization of Particle-Based Reaction-Diffusion Simulations Using MPI.Journal of computational chemistry · 2025Article
- Membrane nanodomains to shape plant cellular functions and signaling.The New phytologist · 2025Review
- The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism.bioRxiv : the preprint server for biology · 2024Article
- Dynamin1 long- and short-tail isoforms exploit distinct recruitment and spatial patterns to form endocytic nanoclusters.Nature communications · 2024Article
- Membrane localization accelerates association under conditions relevant to cellular signaling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Secretion-Catalyzed Assembly of Protein Biomaterials on a Bacterial Membrane Surface.Angewandte Chemie (International ed. in English) · 2023Article
- Temporal control by cofactors prevents kinetic trapping in retroviral Gag lattice assembly.Biophysical journal · 2023Article
- Structure of the HIV immature lattice allows for essential lattice remodeling within budded virions.eLife · 2023Article
- Modeling membrane reshaping driven by dynamic protein assemblies.Current opinion in structural biology · 2023Review
- Large self-assembled clathrin lattices spontaneously disassemble without sufficient adaptor proteins.PLoS computational biology · 2022Article
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2 authors.
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Abstract
Protein assembly is often studied in a three-dimensional solution, but a significant fraction of binding events involve proteins that can reversibly bind and diffuse along a two-dimensional surface. In a recent study, we quantified how proteins can exploit the reduced dimensionality of the membrane to trigger complex formation. Here, we derive a single expression for the characteristic timescale of this multi-step assembly process, where the change in dimensionality renders rates and concentrations effectively time-dependent. We find that proteins can accelerate dimer formation due to an increase in relative concentration, driving more frequent collisions, which often win out over slow-downs due to diffusion. Our model contains two protein populations that dimerize with one another and use a distinct site to bind membrane lipids, creating a complex reaction network. However, by identifying two major rate-limiting pathways to reach an equilibrium steady-state, we derive an excellent approximation for the mean first passage time when lipids are in abundant supply. Our theory highlights how the "sticking rate" or effective adsorption coefficient of the membrane is central in controlling timescales. We also derive a corrected localization rate to quantify how the geometry of the system and diffusion can reduce rates of membrane localization. We validate and test our results using kinetic and particle-based reaction-diffusion simulations. Our results establish how the speed of key assembly steps can shift by orders-of-magnitude when membrane localization is possible, which is critical to understanding mechanisms used in cells.
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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.