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Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL).
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2008 Jun 20; Vol. 283 (25), pp. 17083-91. Date of Electronic Publication: 2008 Apr 22. - Publication Year :
- 2008
-
Abstract
- 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.
- Subjects :
- Antigens chemistry
Asparagine chemistry
Biochemistry methods
Biological Transport
Detergents chemistry
Detergents pharmacology
Humans
Lipids chemistry
Methionine chemistry
Peptide Library
Protein Structure, Tertiary
Static Electricity
Substrate Specificity
Tissue Distribution
ATP-Binding Cassette Transporters chemistry
Peptides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 283
- Issue :
- 25
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 18434309
- Full Text :
- https://doi.org/10.1074/jbc.M801794200