Communications Biology (Dec 2020)

Complimentary action of structured and unstructured domains of epsin supports clathrin-mediated endocytosis at high tension

  • Jophin G. Joseph,
  • Carlos Osorio,
  • Vivian Yee,
  • Ashutosh Agrawal,
  • Allen P. Liu

DOI
https://doi.org/10.1038/s42003-020-01471-6
Journal volume & issue
Vol. 3, no. 1
pp. 1 – 16

Abstract

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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.