ArticleProceedings of the National Academy of Sciences of the United States of America2020
Cooperatively enhanced reactivity and "stabilitaxis" of dissociating oligomeric proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Oxaloacetate sensing promotes innate immune antiviral defence against influenza virus infection.Nature microbiology · 2025Article
- Technology Roadmap of Micro/Nanorobots.ACS nano · 2025Review
- Impact of Ligand-Induced Oligomer Dissociation on Enzyme Diffusion, Directly Observed at the Single-Molecule Level.Nano letters · 2025Article
- Optimized PAR-2 RING dimerization mediates cooperative and selective membrane binding for robust cell polarity.The EMBO journal · 2024Article
- Directing Min protein patterns with advective bulk flow.Nature communications · 2023Article
- Dependence of diffusion ineLife · 2022Article
- Comment on "Relative Diffusivities of Bound and Unbound Protein Can Control Chemotactic Directionality".Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Molecular Diffusivity of Click Reaction Components: The Diffusion Enhancement Question.Journal of the American Chemical Society · 2022Article
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Authors and funding
3 authors.
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Abstract
Many functional units in biology, such as enzymes or molecular motors, are composed of several subunits that can reversibly assemble and disassemble. This includes oligomeric proteins composed of several smaller monomers, as well as protein complexes assembled from a few proteins. By studying the generic spatial transport properties of such proteins, we investigate here whether their ability to reversibly associate and dissociate may confer on them a functional advantage with respect to nondissociating proteins. In uniform environments with position-independent association-dissociation, we find that enhanced diffusion in the monomeric state coupled to reassociation into the functional oligomeric form leads to enhanced reactivity with localized targets. In nonuniform environments with position-dependent association-dissociation, caused by, for example, spatial gradients of an inhibiting chemical, we find that dissociating proteins generically tend to accumulate in regions where they are most stable, a process that we term "stabilitaxis."
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