ArticleNature communications2022
The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Generation and MHC class II loading of an endogenous influenza epitope revealed by a T cell receptor-like antibody.bioRxiv : the preprint server for biology · 2026Article
- Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.Science advances · 2026Article
- Review
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- Interdomain communication in a homodimeric ABC transporter.The Journal of biological chemistry · 2024Article
- Functional Characterization of the Lysosomal Peptide/Histidine Transporter PHT1 (Biomolecules · 2024Article
- Principles of peptide selection by the transporter associated with antigen processing.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.Nature communications · 2024Article
- Reconstitution of ATP-dependent lipid transporters: gaining insight into molecular characteristics, regulation, and mechanisms.Bioscience reports · 2023Review
- Differential Expression ofPharmaceutics · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TAPL is a lysosomal ATP-binding cassette transporter that translocates a broad spectrum of polypeptides from the cytoplasm into the lysosomal lumen. Here we report that, in addition to its well-known role as a peptide translocator, TAPL exhibits an ATP-dependent phosphatidylserine floppase activity that is the possible cause of its high basal ATPase activity and of the lack of coupling between ATP hydrolysis and peptide efflux. We also present the cryo-EM structures of mouse TAPL complexed with (i) phospholipid, (ii) cholesteryl hemisuccinate (CHS) and 9-mer peptide, and (iii) ADP·BeF
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