ArticleThe Journal of biological chemistry2016
Epsin N-terminal Homology Domain (ENTH) Activity as a Function of Membrane Tension.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Recombinant protein platform for high-throughput investigation of peptide-liposome interactions via fluorescence anisotropy depolarization.Communications chemistry · 2026Article
- The Core MICOS Complex Subunit mic60 has Been Substituted by Two Cryptic Mitofilin-containing Proteins in Euglenozoa.Molecular biology and evolution · 2025Article
- Epsin1-mediated exosomal sorting of Dll4 modulates the tubular-macrophage crosstalk in diabetic nephropathy.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- Experimental platform for the functional investigation of membrane proteins in giant unilamellar vesicles.Soft matter · 2022Article
- Article
- Protein-dependent membrane remodeling in mitochondrial morphology and clathrin-mediated endocytosis.European biophysics journal : EBJ · 2021Review
- Cooperativity of membrane-protein and protein-protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis.Cellular and molecular life sciences : CMLS · 2021Article
- Genome-Wide Association Study of Natural Variation inPlants (Basel, Switzerland) · 2021Article
- Complimentary action of structured and unstructured domains of epsin supports clathrin-mediated endocytosis at high tension.Communications biology · 2020Article
- Amphipathic Helices of Cellular Proteins Can Replace the Helix in M2 of Influenza A Virus with Only Small Effects on Virus Replication.Journal of virology · 2020Article
- Physicochemical mechanotransduction alters nuclear shape and mechanics via heterochromatin formation.Molecular biology of the cell · 2019Article
- Epsins Regulate Mouse Embryonic Stem Cell Exit from Pluripotency and Neural Commitment by Controlling Notch Activation.Stem cells international · 2019Article
- Membrane tension increases fusion efficiency of model membranes in the presence of SNAREs.Scientific reports · 2017Article
- The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology.The Journal of cell biology · 2017Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The epsin N-terminal homology domain (ENTH) is a major player in clathrin-mediated endocytosis. To investigate the influence of initial membrane tension on ENTH binding and activity, we established a bilayer system based on adhered giant unilamellar vesicles (GUVs) to be able to control and adjust the membrane tension σ covering a broad regime. The shape of each individual adhered GUV as well as its adhesion area was monitored by spinning disc confocal laser microscopy. Control of σ in a range of 0.08-1.02 mN/m was achieved by altering the Mg(2+) concentration in solution, which changes the surface adhesion energy per unit area of the GUVs. Specific binding of ENTH to phosphatidylinositol 4,5-bisphosphate leads to a substantial increase in adhesion area of the sessile GUV. At low tension (<0.1 mN/m) binding of ENTH can induce tubular structures, whereas at higher membrane tension the ENTH interaction deflates the sessile GUV and thereby increases the adhesion area. The increase in adhesion area is mainly attributed to a decrease in the area compressibility modulus KA We propose that the insertion of the ENTH helix-0 into the membrane is largely responsible for the observed decrease in KA, which is supported by the observation that the mutant ENTH L6E shows a reduced increase in adhesion area. These results demonstrate that even in the absence of tubule formation, the area compressibility modulus and, as such, the bending rigidity of the membrane is considerably reduced upon ENTH binding. This renders membrane bending and tubule formation energetically less costly.
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