Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter

Science. 1993 Aug 6;261(5122):769-71. doi: 10.1126/science.8342042.

Abstract

Major histocompatibility complex (MHC) class I molecules present peptides derived from nuclear and cytosolic proteins to CD8+ T cells. These peptides are translocated into the lumen of the endoplasmic reticulum (ER) to associate with class I molecules. Two MHC-encoded putative transporter proteins, TAP1 and TAP2, are required for efficient assembly of class I molecules and presentation of endogenous peptides. Expression of TAP1 and TAP2 in a mutant cell line resulted in the delivery of an 11-amino acid oligomer model peptide to the ER. Peptide translocation depended on the sequence of the peptide, was adenosine triphosphate (ATP)-dependent, required ATP hydrolysis, and was inhibited in a concentration-dependent manner.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 2
  • ATP Binding Cassette Transporter, Subfamily B, Member 3
  • ATP-Binding Cassette Transporters*
  • Adenosine Triphosphate / metabolism*
  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Membrane Permeability
  • Endoplasmic Reticulum / metabolism
  • Glycosylation
  • Histocompatibility Antigens Class II / metabolism*
  • Molecular Sequence Data
  • Oligopeptides / metabolism*
  • Rats
  • T-Lymphocytes, Cytotoxic / metabolism*
  • Transfection

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 2
  • ATP Binding Cassette Transporter, Subfamily B, Member 3
  • ATP-Binding Cassette Transporters
  • Carrier Proteins
  • Histocompatibility Antigens Class II
  • Oligopeptides
  • TAP1 protein, human
  • Tap1 protein, rat
  • Tap2 protein, rat
  • TAP2 protein, human
  • Adenosine Triphosphate