Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)

Justina Clarinda Wolters, Rupert Abele, Robert Tampé

Research output: Contribution to journalArticleAcademicpeer-review

52 Citations (Scopus)

Abstract

The transporter associated with antigen processing (TAP)-like (TAPL, ABCB9) belongs to the ATP-binding cassette transporter family, which translocates a vast variety of solutes across membranes. The function of this half-size transporter has not yet been determined. Here, we show that TAPL forms a homodimeric complex, which translocates peptides across the membrane. Peptide transport strictly requires ATP hydrolysis. The transport follows Michaelis-Menten kinetics with low affinity and high capacity. Different nucleotides bind and energize the transport with a slight predilection for purine bases. The peptide specificity is very broad, ranging from 6-mer up to at least 59-mer peptides with a preference for 23-mers. Peptides are recognized via their backbone, including the free N and C termini as well as side chain interactions. Although related to TAP, TAPL is unique as far as its interaction partners, transport properties, and substrate specificities are concerned, thus excluding that TAPL is part of the peptide-loading complex in the classic route of antigen processing via major histocompatibility complex class I molecules.

Original languageEnglish
Pages (from-to)23631-6
Number of pages6
JournalThe Journal of Biological Chemistry
Volume280
Issue number25
DOIs
Publication statusPublished - 24-Jun-2005
Externally publishedYes

Keywords

  • ATP-Binding Cassette Transporters
  • Adenosine Triphosphate
  • Base Sequence
  • DNA Primers
  • Dimerization
  • Humans
  • Kinetics
  • Peptides
  • Protein Transport

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