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    ABCB9 ATP binding cassette subfamily B member 9 [ Homo sapiens (human) ]

    Gene ID: 23457, updated on 17-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    results expand our knowledge about lysosomal trafficking of TAPL and the general function of extra transmembrane domains of ABC transporters

    Lysosomal targeting of the ABC transporter TAPL is determined by membrane-localized charged residues.
    Graab P, Bock C, Weiss K, Hirth A, Koller N, Braner M, Jung J, Loehr F, Tampé R, Behrends C, Abele R., Free PMC Article

    01/11/2020
    the TMD0 of TAPL was expressed via a cell-free expression system and confirmed its correct folding by NMR and interaction studies.

    Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL.
    Bock C, Löhr F, Tumulka F, Reichel K, Würz J, Hummer G, Schäfer L, Tampé R, Joseph B, Bernhard F, Dötsch V, Abele R., Free PMC Article

    11/23/2019
    The structure of the unique domain of TAPL, is reported.

    Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
    Tumulka F, Roos C, Löhr F, Bock C, Bernhard F, Dötsch V, Abele R.

    05/24/2014
    LAMP proteins retain TAPL on the limiting membrane of endosomes and prevent its sorting to intraluminal vesicles.

    The lysosomal polypeptide transporter TAPL is stabilized by interaction with LAMP-1 and LAMP-2.
    Demirel Ö, Jan I, Wolters D, Blanz J, Saftig P, Tampé R, Abele R.

    04/27/2013
    These results suggest that TAPL may be localized to the microdomains (lipid rafts) of lysosomal membranes enriched in cholesterol.

    Transporter associated with antigen processing-like (ABCB9) stably expressed in Chinese hamster ovary-K1 cells is sorted to the microdomains of lysosomal membranes.
    Fujimoto Y, Kamakura A, Motohashi Y, Ohashi-Kobayashi A, Maeda M.

    05/21/2011
    By dissecting ABCB9, distinct functions were assigned to the core complex and the extra N-terminal transmembrane domain.

    Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain.
    Demirel O, Bangert I, Tampé R, Abele R.

    08/9/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Association study between single-nucleotide polymorphisms in 199 drug-related genes and commonly measured quantitative traits of 752 healthy Japanese subjects.
    Saito A, Kawamoto M, Kamatani N.

    04/29/2009
    These results suggest that the sorting signal for lysosomes is present within the amino-terminal transmembrane domain (Met(1)-Arg(141)) of the TAPL molecule.

    Functional dissection of transmembrane domains of human TAP-like (ABCB9).
    Kamakura A, Fujimoto Y, Motohashi Y, Ohashi K, Ohashi-Kobayashi A, Maeda M.

    01/21/2010
    analysis of lipid activation of the lysosomal transport complex ABCB9

    Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL).
    Zhao C, Haase W, Tampé R, Abele R.

    01/21/2010
    the TAPL-specific translocation of peptides into isolated lysosomes strictly requires ATP hydrolysis

    Identification of a lysosomal peptide transport system induced during dendritic cell development.
    Demirel O, Waibler Z, Kalinke U, Grünebach F, Appel S, Brossart P, Hasilik A, Tampé R, Abele R.

    01/21/2010
    The ATP-binding of TAPL required Mg(2+), and was observed at neutral pH. Chemical cross-linking experiments suggested that TAPL forms a homodimer in the membrane and under the solubilized conditions.

    Biochemical characterization of transporter associated with antigen processing (TAP)-like (ABCB9) expressed in insect cells.
    Ohara T, Ohashi-Kobayashi A, Maeda M.

    01/21/2010
    is part of the peptide-loading complex in the classic route of antigen processing via major histocompatibility complex class I molecules

    Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9).
    Wolters JC, Abele R, Tampé R.

    01/21/2010
    These findings suggest that the transport activity of hTAPL is important for conferring high valinomycin-sensitive phenotype to yeast.

    Examination of drug resistance activity of human TAP-like (ABCB9) expressed in yeast.
    Ohashi-Kobayashi A, Ohashi K, Du WB, Omote H, Nakamoto R, Al-Shawi M, Maeda M.

    01/21/2010
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