ArticleProceedings of the National Academy of Sciences of the United States of America1997
Cloning and functional characterization of a subunit of the transporter associated with antigen processing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 122 citations in OpenAlex.
- Genetic characterization of the TAPBP and its allelic association with BF2 in the chicken major histocompatibility complex.Immunogenetics · 2026Article
- Chaperone function in antigen presentation by MHC class I molecules-tapasin in the PLC and TAPBPR beyond.Frontiers in immunology · 2023Review
- Atlantic cod (Frontiers in cell and developmental biology · 2023Article
- Article
- Preferential interaction of MHC class I with TAPBPR in the absence of glycosylation.Molecular immunology · 2019Article
- A personal retrospective on the mechanisms of antigen processing.Immunogenetics · 2019Review
- Utilizing TAPBPR to promote exogenous peptide loading onto cell surface MHC I molecules.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.The Journal of biological chemistry · 2017Article
- Article
- Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.Frontiers in immunology · 2017Review
- TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst.eLife · 2015Article
- Distinct assembly profiles of HLA-B molecules.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- TAPBPR isoforms exhibit altered association with MHC class I.Immunology · 2014Article
- The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complex.Cellular and molecular life sciences : CMLS · 2012Article
- Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.The Journal of biological chemistry · 2012Article
- Lsr2 peptides of Mycobacterium leprae show hierarchical responses in lymphoproliferative assays, with selective recognition by patients with anergic lepromatous leprosy.Infection and immunity · 2012Article
- Tapasin discriminates peptide-human leukocyte antigen-A*02:01 complexes formed with natural ligands.The Journal of biological chemistry · 2011Article
- Identification of an alternate splice form of tapasin in human melanoma.Human immunology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transporter associated with antigen processing (TAP) is essential for the transport of antigenic peptides across the membrane of the endoplasmic reticulum. In addition, TAP interacts with major histocompatibility complex class I heavy chain (HC)/beta2-microglobulin (beta2-m) dimers. We have cloned a cDNA encoding a TAP1/2-associated protein (TAP-A) corresponding in size and biochemical properties to tapasin, which was recently suggested to be involved in class I-TAP interaction (Sadasivan, B., Lehner, P. J., Ortmann, B., Spies, T. & Cresswell, P. (1996) Immunity 5, 103-114). The cDNA encodes a 448-residue-long ORF, including a signal peptide. The protein is predicted to be a type I membrane glycoprotein with a cytoplasmic tail containing a double-lysine motif (-KKKAE-COOH) known to maintain membrane proteins in the endoplasmic reticulum. Immunoprecipitation with anti-TAP1 or anti-TAP-A antisera demonstrated a consistent and stoichiometric association of TAP-A with TAP1/2. Class I HC and beta2-m also were coprecipitated with these antisera, indicating the presence of a pentameric complex. In pulse-chase experiments, class I HC/beta2-m rapidly dissociated from TAP1/2-TAP-A. We propose that TAP is a trimeric complex consisting of TAP1, TAP2, and TAP-A that interacts transiently with class I HC/beta2-m. In peptide-binding assays using cross-linkable peptides and intact microsomes, TAP-A bound peptides only in the presence of ATP whereas binding of peptides to TAP1/2 was ATP-independent. This suggests a direct role of TAP-A in peptide loading onto class I HC/beta2-m dimer.
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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.