ArticleBiophysical journal2014
Membrane fluctuations destabilize clathrin protein lattice order.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Membrane bending energy selects for compact growth of protein assemblies.bioRxiv : the preprint server for biology · 2025Article
- Large self-assembled clathrin lattices spontaneously disassemble without sufficient adaptor proteins.PLoS computational biology · 2022Article
- Protein crowding mediates membrane remodeling in upstream ESCRT-induced formation of intraluminal vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Why Enveloped Viruses Need Cores-The Contribution of a Nucleocapsid Core to Viral Budding.Biophysical journal · 2018Article
- Membrane perturbing properties of toxin mycolactone from Mycobacterium ulcerans.PLoS computational biology · 2018Article
- Clathrin polymerization exhibits high mechano-geometric sensitivity.Soft matter · 2017Article
- Clathrin Assembly Regulated by Adaptor Proteins in Coarse-Grained Models.Biophysical journal · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We develop a theoretical model of a clathrin protein lattice on a flexible cell membrane. The clathrin subunit is modeled as a three-legged pinwheel with elastic deformation modes and intersubunit binding interactions. The pinwheels are constrained to lie on the surface of an elastic sheet that opposes bending deformation and is subjected to tension. Through Monte Carlo simulations, we predict the equilibrium phase behavior of clathrin lattices at various levels of tension. High membrane tensions, which correspond to suppressed membrane fluctuations, tend to stabilize large, flat crystalline structures similar to plaques that have been observed in vivo on cell membranes that are adhered to rigid surfaces. Low tensions, on the other hand, give rise to disordered, defect-ridden lattices that behave in a fluidlike manner. The principles of two-dimensional melting theory are applied to our model system to further clarify how high tensions can stabilize crystalline order on flexible membranes. These results demonstrate the importance of environmental physical cues in dictating the collective behavior of self-assembled protein structures.
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