TY  - JOUR
A1  - Zhao, Chenguang
A1  - Haase, Winfried
A1  - Tampé, Robert
A1  - Abele, Rupert
T1  - Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL)
T2  - Journal of biological chemistry
N2  - The lysosomal ABC transporter associated with antigen processing-like (TAPL, ABCB9) acts as an ATP-dependent polypeptide transporter with broad length selectivity. To characterize in detail its substrate specificity, a procedure for functional reconstitution of human TAPL was developed. By intensive screening of detergents, ideal solubilization conditions were evolved with respect to efficiency, long term stability, and functionality of TAPL. TAPL was isolated in a two-step procedure with high purity and, subsequently, reconstituted into proteoliposomes. The peptide transport activity of reconstituted TAPL strongly depends on the lipid composition. With the help of combinatorial peptide libraries, the key positions of the peptides were localized to the N- and C-terminal residues with respect to peptide transport. At both ends, TAPL favors positively charged, aromatic, or hydrophobic residues and disfavors negatively charged residues as well as asparagine and methionine. Besides specific interactions of both terminal residues, electrostatic interactions are important, since peptides with positive net charge are more efficiently transported than negatively charged ones.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76338
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-763386
SN  - 0021-9258
VL  - 283
IS  - 25
SP  - 17083
EP  - 17091
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -