Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors

J Biol Chem. 1998 Jan 23;273(4):1847-50. doi: 10.1074/jbc.273.4.1847.

Abstract

Eps15 is a phosphorylation substrate of the epidermal growth factor receptor kinase. In vivo, it is largely found in complex with AP-2, the plasma membrane clathrin adaptor protein complex. Although AP-2 is uniformly distributed across the surface of clathrin-coated pits and vesicles, Eps15 is preferentially found in the rims of endocytic clathrin-coated pits (1). This observation suggests that Eps15 may disengage from AP-2 during coat formation. Here we use two new anti-Eps15 antibodies to show that, contrary to our own earlier suggestion, coated vesicles isolated from brain do not contain detectable amounts of Eps15. Furthermore, when AP-2 complexes that are saturated with Eps15 are used for in vitro assembly of clathrin-AP-2 coats, normal structures are formed that contain the expected amounts of clathrin and AP-2, but the amount of Eps15 present is dramatically lower than that of AP-2. We propose that during coated pit formation, addition of clathrin to the growing edge at the rim of the pit releases Eps15 from AP-2.

Publication types

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

MeSH terms

  • Adaptor Protein Complex alpha Subunits
  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Brain Chemistry
  • Calcium-Binding Proteins / metabolism*
  • Cattle
  • Clathrin / metabolism*
  • Coated Pits, Cell-Membrane / metabolism
  • Coated Pits, Cell-Membrane / ultrastructure
  • Macromolecular Substances
  • Membrane Proteins / metabolism*
  • Microscopy, Electron
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Signal Transduction*

Substances

  • Adaptor Protein Complex alpha Subunits
  • Adaptor Proteins, Vesicular Transport
  • Calcium-Binding Proteins
  • Clathrin
  • Macromolecular Substances
  • Membrane Proteins
  • Phosphoproteins
  • Recombinant Proteins