TAP and TAP-like — Brothers in arms?
Identifieur interne : 001175 ( Istex/Corpus ); précédent : 001174; suivant : 001176TAP and TAP-like — Brothers in arms?
Auteurs : Chenguang Zhao ; Robert Tampé ; Rupert AbeleSource :
- Naunyn-Schmiedeberg's Archives of Pharmacology [ 0028-1298 ] ; 2006-03-01.
English descriptors
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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
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<front><div type="abstract" xml: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.</div>
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<Para>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.</Para>
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<Description><Para>ATP-binding cassette</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>ER</Term>
<Description><Para>endoplasmic reticulum</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>MHC</Term>
<Description><Para>major histocompatibility complex</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>NBD</Term>
<Description><Para>nucleotide binding domain</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>TAP</Term>
<Description><Para>transporter associated with antigen processing</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>TAPL</Term>
<Description><Para>transporter associated with antigen processing like</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>TMD</Term>
<Description><Para>transmembrane domain</Para>
</Description>
</DefinitionListEntry>
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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>
<note>Review</note>
<subject lang="en"><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>
</subject>
<subject></subject>
<relatedItem type="host"><titleInfo><title>Naunyn-Schmiedeberg's Archives of Pharmacology</title>
</titleInfo>
<titleInfo type="abbreviated"><title>Naunyn-Schmied Arch Pharmacol</title>
</titleInfo>
<genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre>
<originInfo><publisher>Springer</publisher>
<dateIssued encoding="w3cdtf">2006-03-20</dateIssued>
<copyrightDate encoding="w3cdtf">2006</copyrightDate>
</originInfo>
<identifier type="ISSN">0028-1298</identifier>
<identifier type="eISSN">1432-1912</identifier>
<identifier type="JournalID">210</identifier>
<identifier type="IssueArticleCount">8</identifier>
<identifier type="VolumeIssueCount">6</identifier>
<part><date>2006</date>
<detail type="issue"><title>Special Issue: Transporters</title>
</detail>
<detail type="volume"><number>372</number>
<caption>vol.</caption>
</detail>
<detail type="issue"><number>6</number>
<caption>no.</caption>
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<extent unit="pages"><start>444</start>
<end>450</end>
</extent>
</part>
<recordInfo><recordOrigin>Springer-Verlag, 2006</recordOrigin>
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<identifier type="istex">D19D4A8965778A8A641C70D234C08919437A1713</identifier>
<identifier type="ark">ark:/67375/VQC-R0D2S84W-M</identifier>
<identifier type="DOI">10.1007/s00210-005-0028-z</identifier>
<identifier type="ArticleID">28</identifier>
<identifier type="ArticleID">s00210-005-0028-z</identifier>
<accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2006</accessCondition>
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