Complimentary action of structured and unstructured domains of epsin supports clathrin-mediated endocytosis at high tension
Using imaging and molecular dynamics simulations, Joseph et al characterize the tension-responsive recruitment of the membrane bending protein epsin and its stabilization of clathrin-coated structures (CCSs) to form clathrin-coated pits. They find epsin’s ENTH- and unstructured IDP domains play comp...
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| Autores principales: | , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2020
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/af160bb607ba4d5e9eee489c34d49af9 |
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| Sumario: | Using imaging and molecular dynamics simulations, Joseph et al characterize the tension-responsive recruitment of the membrane bending protein epsin and its stabilization of clathrin-coated structures (CCSs) to form clathrin-coated pits. They find epsin’s ENTH- and unstructured IDP domains play complementary roles in CCS maturation under high tension. |
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