Interaction of tyrosine-based sorting signals with clathrin-associated proteins

Science. 1995 Sep 29;269(5232):1872-5. doi: 10.1126/science.7569928.

Abstract

Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains (mu 1 and mu 2) of two clathrin-associated protein complexes (AP-1 and AP-2, respectively) specifically interacted with tyrosine-based signals of several integral membrane proteins. The interaction was confirmed by in vitro binding assays. Thus, it is likely that the medium chains serve as signal-binding components of the clathrin-dependent sorting machinery.

Publication types

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

MeSH terms

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Cell Membrane / metabolism
  • Clathrin / metabolism*
  • Cloning, Molecular
  • Glutathione Transferase / metabolism
  • Golgi Apparatus / metabolism
  • Lysosomes / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Protein Sorting Signals / chemistry
  • Protein Sorting Signals / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Transformation, Genetic
  • Tyrosine / metabolism*

Substances

  • Adaptor Proteins, Vesicular Transport
  • Clathrin
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Protein Sorting Signals
  • Recombinant Fusion Proteins
  • Tyrosine
  • Glutathione Transferase

Associated data

  • GENBANK/U27106