TY  - JOUR
A1  - Wolters, Justina Clarinda
A1  - Abele, Rupert
A1  - Tampé, Robert
T1  - Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
T2  - Journal of biological chemistry
N2  - 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.
Y1  - 2005
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76194
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-761941
SN  - 0021-9258
VL  - 280
IS  - 25
SP  - 23631
EP  - 23636
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -