The mu2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and YppØ sorting signals at distinct sites

Traffic. 2002 Aug;3(8):590-600. doi: 10.1034/j.1600-0854.2002.30808.x.

Abstract

The endocytic sorting signal on the low-density lipoprotein receptor for clathrin-mediated internalization is the sequence FDNPVY in the receptor's cytosolic tail. We have used a combination of surface plasmon resonance and crosslinking with a photoactivated peptide probe to demonstrate the interaction between FDNPVY-containing peptides and the mu2 chain of purified AP-2 clathrin adaptors (the complexes responsible for plasma membrane sorting). We show that recognition of the FDNPVY signal is mediated by a binding site in the mu2-subunit that is distinct from the site for the more general YppØ sorting signal, another tyrosine-based sequence also recognized by mu2-adaptin. These results suggest the possibility that low-density lipoprotein receptor uptake may be modulated specifically and independently of other proteins in the clathrin pathway.

Publication types

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

MeSH terms

  • Adaptor Protein Complex 2 / chemistry*
  • Adaptor Protein Complex 2 / genetics
  • Adaptor Protein Complex 2 / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Endocytosis
  • In Vitro Techniques
  • Kinetics
  • Molecular Sequence Data
  • Protein Binding
  • Protein Subunits
  • Receptors, LDL / chemistry
  • Receptors, LDL / genetics
  • Receptors, LDL / metabolism
  • Signal Transduction

Substances

  • Adaptor Protein Complex 2
  • Protein Subunits
  • Receptors, LDL