ArticleThe Biochemical journal2015
Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Integrating Single-Cell and Bulk RNA Sequencing Data to Explore Sphingolipid Metabolism Molecular Signatures in Ovarian Cancer Prognosis: an Original Study.International journal of medical sciences · 2025Article
- The role of ATP-binding Cassette subfamily B member 6 in the inner ear.Nature communications · 2024Article
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- Cryo-EM structure of cadmium-bound human ABCB6.Communications biology · 2024Article
- Drug resistance mechanisms in cancers: Execution of pro-survival strategies.Journal of biomedical research · 2024Article
- Structural View of Cryo-Electron Microscopy-Determined ATP-Binding Cassette Transporters in Human Multidrug Resistance.Biomolecules · 2024Review
- Identification of two novel heterodimeric ABC transporters in melanoma: ABCB5β/B6 and ABCB5β/B9.The Journal of biological chemistry · 2024Article
- W546 stacking disruption traps the human porphyrin transporter ABCB6 in an outward-facing transient state.Communications biology · 2023Article
- Structural Insights into Porphyrin Recognition by the Human ATP-Binding Cassette Transporter ABCB6.Molecules and cells · 2022Article
- Melanosome Biogenesis in the Pigmentation of Mammalian Skin.Integrative and comparative biology · 2021Review
- Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cryo-electron microscopy structure of human ABCB6 transporter.Protein science : a publication of the Protein Society · 2020Article
- Sequence Features of Mitochondrial Transporter Protein Families.Biomolecules · 2020Review
- Linker Domains: Why ABC Transporters 'Live in Fragments no Longer'.Trends in biochemical sciences · 2020Review
- The human ABCB6 protein is the functional homologue of HMT-1 proteins mediating cadmium detoxification.Cellular and molecular life sciences : CMLS · 2019Article
- Chronic Pressure Overload Results in Deficiency of Mitochondrial Membrane Transporter ABCB7 Which Contributes to Iron Overload, Mitochondrial Dysfunction, Metabolic Shift and Worsens Cardiac Function.Scientific reports · 2019Article
- Application of antihelix antibodies in protein structure determination.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Lysosomal targeting of the ABC transporter TAPL is determined by membrane-localized charged residues.The Journal of biological chemistry · 2019Article
- Mitochondrial membrane transporters and metabolic switch in heart failure.Heart failure reviews · 2019Review
- Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL.Scientific reports · 2018Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
ATP-binding cassette, subfamily B (ABCB) 6 is a homodimeric ATP-binding cassette (ABC) transporter present in the plasma membrane and in the intracellular organelles. The intracellular localization of ABCB6 has been a matter of debate, as it has been suggested to reside in the mitochondria and the endo-lysosomal system. Using a variety of imaging modalities, including confocal microscopy and EM, we confirm the endo-lysosomal localization of ABCB6 and show that the protein is internalized from the plasma membrane through endocytosis, to be distributed to multivesicular bodies and lysosomes. In addition to the canonical nucleotide-binding domain (NBD) and transmembrane domain (TMD), ABCB6 contains a unique N-terminal TMD (TMD0), which does not show sequence homology to known proteins. We investigated the functional role of these domains through the molecular dissection of ABCB6. We find that the folding, dimerization, membrane insertion and ATP binding/hydrolysis of the core-ABCB6 complex devoid of TMD0 are preserved. However, in contrast with the full-length transporter, the core-ABCB6 construct is retained at the plasma membrane and does not appear in Rab5-positive endosomes. TMD0 is directly targeted to the lysosomes, without passage to the plasma membrane. Collectively, our results reveal that TMD0 represents an independently folding unit, which is dispensable for catalysis, but has a crucial role in the lysosomal targeting of ABCB6.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.