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TAP and TAP-like — Brothers in arms?

Identifieur interne : 001175 ( Istex/Corpus ); précédent : 001174; suivant : 001176

TAP and TAP-like — Brothers in arms?

Auteurs : Chenguang Zhao ; Robert Tampé ; Rupert Abele

Source :

RBID : ISTEX:D19D4A8965778A8A641C70D234C08919437A1713

English descriptors

Abstract

Abstract: The transporter associated with antigen processing like (TAPL, ABCB9) is a member of the ATP-binding cassette (ABC) transporter family. Moreover, TAPL belongs to the TAP family due to its high sequence homology to TAP1 and TAP2. TAPL forms a homodimer which is localized in lysosomes with a minor fraction in the ER. It functions as an ATP-dependent peptide transporter which shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. In contrast to TAP, TAPL transports peptides with low affinity but high efficiency. This review will briefly summarize current knowledge about the structural organization and possible physiological function of TAPL in antigen processing and presentation.

Url:
DOI: 10.1007/s00210-005-0028-z

Links to Exploration step

ISTEX:D19D4A8965778A8A641C70D234C08919437A1713

Le document en format XML

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<DefinitionListEntry>
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<Para>endoplasmic reticulum</Para>
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<DefinitionListEntry>
<Term>NBD</Term>
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<Para>nucleotide binding domain</Para>
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<DefinitionListEntry>
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<Description>
<Para>transporter associated with antigen processing</Para>
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<Para>transporter associated with antigen processing like</Para>
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<DefinitionListEntry>
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</Description>
</DefinitionListEntry>
</DefinitionList>
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<namePart type="family">Zhao</namePart>
<affiliation>Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie-Str. 9, 60439, Frankfurt am Main, Germany</affiliation>
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<namePart type="given">Robert</namePart>
<namePart type="family">Tampé</namePart>
<affiliation>Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie-Str. 9, 60439, Frankfurt am Main, Germany</affiliation>
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<namePart type="given">Rupert</namePart>
<namePart type="family">Abele</namePart>
<affiliation>Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie-Str. 9, 60439, Frankfurt am Main, Germany</affiliation>
<affiliation>E-mail: abele@em.uni-frankfurt.de</affiliation>
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<abstract lang="en">Abstract: The transporter associated with antigen processing like (TAPL, ABCB9) is a member of the ATP-binding cassette (ABC) transporter family. Moreover, TAPL belongs to the TAP family due to its high sequence homology to TAP1 and TAP2. TAPL forms a homodimer which is localized in lysosomes with a minor fraction in the ER. It functions as an ATP-dependent peptide transporter which shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. In contrast to TAP, TAPL transports peptides with low affinity but high efficiency. This review will briefly summarize current knowledge about the structural organization and possible physiological function of TAPL in antigen processing and presentation.</abstract>
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<genre>Keywords</genre>
<topic>ABC transporter</topic>
<topic>ABCB9</topic>
<topic>Adaptive immunity</topic>
<topic>Antigen processing</topic>
<topic>Lysosome</topic>
<topic>Peptide transporter</topic>
<topic>TAP family</topic>
<topic>Transport assay</topic>
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<title>Naunyn-Schmiedeberg's Archives of Pharmacology</title>
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<dateIssued encoding="w3cdtf">2006-03-20</dateIssued>
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<identifier type="ISSN">0028-1298</identifier>
<identifier type="eISSN">1432-1912</identifier>
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<title>Special Issue: Transporters</title>
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<caption>vol.</caption>
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<number>6</number>
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<start>444</start>
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<identifier type="DOI">10.1007/s00210-005-0028-z</identifier>
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