Epsin: inducing membrane curvature

Int J Biochem Cell Biol. 2007;39(10):1765-70. doi: 10.1016/j.biocel.2006.12.004. Epub 2007 Jan 17.


Epsin was originally discovered by virtue of its binding to another accessory protein, Eps15. Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. Epsin isoforms have been described that differ in intracellular site of action and/or in tissue distribution, although all epsins essentially contribute to membrane deformation. Besides inducing membrane curvature, epsin also plays a key function as adaptor protein, coupling various components of the clathrin-assisted uptake and fulfils an important role in selecting and recognizing cargo. Furthermore, epsin possesses the ability to block vesicle formation during mitosis. To perform all these functions, epsin, apart from interacting with PtdIns(4,5)P2 via its ENTH domain, also engages in several protein interactions with different components of the clathrin-mediated endocytic system. Recently, RNA interference has successfully been exploited to generate a cell line constitutively silencing epsin expression, which can be used to study internalization of multiple ligands.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Vesicular Transport / genetics
  • Adaptor Proteins, Vesicular Transport / physiology*
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / physiology*
  • Coated Pits, Cell-Membrane / metabolism*
  • Gene Expression Regulation
  • Humans
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid


  • Adaptor Proteins, Vesicular Transport
  • epsin