Characterization of a Di-leucine–based Signal in the Cytoplasmic Tail of the Nucleotide-pyrophosphatase NPP1 That Mediates Basolateral Targeting but not Endocytosis
Identifieur interne : 000988 ( Pmc/Curation ); précédent : 000987; suivant : 000989Characterization of a Di-leucine–based Signal in the Cytoplasmic Tail of the Nucleotide-pyrophosphatase NPP1 That Mediates Basolateral Targeting but not Endocytosis
Auteurs : Valérie Bello [France] ; James W. Goding [Australie] ; Vicki Greengrass [Australie] ; Adnan Sali [Australie] ; Valentina Dubljevic [Australie] ; Christelle Lenoir [France] ; Germain Trugnan [France] ; Michèle Maurice [France]Source :
- Molecular Biology of the Cell [ 1059-1524 ] ; 2001.
Abstract
Enzymes of the nucleotide pyrophosphatase/phosphodiesterase (NPPase) family are expressed at opposite surfaces in polarized epithelial cells. We investigated the targeting signal of NPP1, which is exclusively expressed at the basolateral surface. Full-length NPP1 and different constructs and mutants were transfected into the polarized MDCK cell line. Expression of the proteins was analyzed by confocal microscopy and surface biotinylation. The basolateral signal of NPP1 was identified as a di-leucine motif located in the cytoplasmic tail. Mutation of either or both leucines largely redirected NPP1 to the apical surface. Furthermore, addition of the conserved sequence AAASLLAP redirected the apical nucleotide pyrophosphatase/phosphodiesterase NPP3 to the basolateral surface. Full-length NPP1 was not significantly internalized. However, when the cytoplasmic tail was deleted upstream the di-leucine motif or when the six upstream flanking amino acids were deleted, the protein was mainly found intracellularly. Endocytosis experiments indicated that these mutants were endocytosed from the basolateral surface. These results identify the basolateral signal of NPP1 as a short sequence including a di-leucine motif that is dominant over apical determinants and point to the importance of surrounding amino acids in determining whether the signal will function as a basolateral signal only or as an endocytotic signal as well.
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PubMed: 11598187
PubMed Central: 60151
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Goding</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Greengrass, Vicki" sort="Greengrass, Vicki" uniqKey="Greengrass V" first="Vicki" last="Greengrass">Vicki Greengrass</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Sali, Adnan" sort="Sali, Adnan" uniqKey="Sali A" first="Adnan" last="Sali">Adnan Sali</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Dubljevic, Valentina" sort="Dubljevic, Valentina" uniqKey="Dubljevic V" first="Valentina" last="Dubljevic">Valentina Dubljevic</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Lenoir, Christelle" sort="Lenoir, Christelle" uniqKey="Lenoir C" first="Christelle" last="Lenoir">Christelle Lenoir</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author><author><name sortKey="Trugnan, Germain" sort="Trugnan, Germain" uniqKey="Trugnan G" first="Germain" last="Trugnan">Germain Trugnan</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author><author><name sortKey="Maurice, Michele" sort="Maurice, Michele" uniqKey="Maurice M" first="Michèle" last="Maurice">Michèle Maurice</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">11598187</idno><idno type="pmc">60151</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC60151</idno><idno type="RBID">PMC:60151</idno><date when="2001">2001</date><idno type="wicri:Area/Pmc/Corpus">000A11</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000A11</idno><idno type="wicri:Area/Pmc/Curation">000988</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000988</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Characterization of a Di-leucine–based Signal in the Cytoplasmic Tail of the Nucleotide-pyrophosphatase NPP1 That Mediates Basolateral Targeting but not Endocytosis</title><author><name sortKey="Bello, Valerie" sort="Bello, Valerie" uniqKey="Bello V" first="Valérie" last="Bello">Valérie Bello</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author><author><name sortKey="Goding, James W" sort="Goding, James W" uniqKey="Goding J" first="James W." last="Goding">James W. Goding</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Greengrass, Vicki" sort="Greengrass, Vicki" uniqKey="Greengrass V" first="Vicki" last="Greengrass">Vicki Greengrass</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Sali, Adnan" sort="Sali, Adnan" uniqKey="Sali A" first="Adnan" last="Sali">Adnan Sali</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Dubljevic, Valentina" sort="Dubljevic, Valentina" uniqKey="Dubljevic V" first="Valentina" last="Dubljevic">Valentina Dubljevic</name><affiliation wicri:level="1"><nlm:aff id="N0x9ed5310.0x8bab9b8">Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181</wicri:regionArea></affiliation></author><author><name sortKey="Lenoir, Christelle" sort="Lenoir, Christelle" uniqKey="Lenoir C" first="Christelle" last="Lenoir">Christelle Lenoir</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author><author><name sortKey="Trugnan, Germain" sort="Trugnan, Germain" uniqKey="Trugnan G" first="Germain" last="Trugnan">Germain Trugnan</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author><author><name sortKey="Maurice, Michele" sort="Maurice, Michele" uniqKey="Maurice M" first="Michèle" last="Maurice">Michèle Maurice</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x9ed5310.0x8bab9b8">U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12</wicri:regionArea></affiliation></author></analytic><series><title level="j">Molecular Biology of the Cell</title><idno type="ISSN">1059-1524</idno><imprint><date when="2001">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Enzymes of the nucleotide pyrophosphatase/phosphodiesterase (NPPase) family are expressed at opposite surfaces in polarized epithelial cells. We investigated the targeting signal of NPP1, which is exclusively expressed at the basolateral surface. Full-length NPP1 and different constructs and mutants were transfected into the polarized MDCK cell line. Expression of the proteins was analyzed by confocal microscopy and surface biotinylation. The basolateral signal of NPP1 was identified as a di-leucine motif located in the cytoplasmic tail. Mutation of either or both leucines largely redirected NPP1 to the apical surface. Furthermore, addition of the conserved sequence AAASLLAP redirected the apical nucleotide pyrophosphatase/phosphodiesterase NPP3 to the basolateral surface. Full-length NPP1 was not significantly internalized. However, when the cytoplasmic tail was deleted upstream the di-leucine motif or when the six upstream flanking amino acids were deleted, the protein was mainly found intracellularly. Endocytosis experiments indicated that these mutants were endocytosed from the basolateral surface. These results identify the basolateral signal of NPP1 as a short sequence including a di-leucine motif that is dominant over apical determinants and point to the importance of surrounding amino acids in determining whether the signal will function as a basolateral signal only or as an endocytotic signal as well.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Mol Biol Cell</journal-id><journal-id journal-id-type="publisher-id">MOL BIOL CELL</journal-id><journal-title>Molecular Biology of the Cell</journal-title><issn pub-type="ppub">1059-1524</issn><publisher><publisher-name>The American Society for Cell Biology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">11598187</article-id><article-id pub-id-type="pmc">60151</article-id><article-id pub-id-type="publisher-id">1625</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Characterization of a Di-leucine–based Signal in the Cytoplasmic Tail of the Nucleotide-pyrophosphatase NPP1 That Mediates Basolateral Targeting but not Endocytosis</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bello</surname><given-names>Valérie</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">*</xref></contrib><contrib contrib-type="author"><name><surname>Goding</surname><given-names>James W.</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">†</xref></contrib><contrib contrib-type="author"><name><surname>Greengrass</surname><given-names>Vicki</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">†</xref></contrib><contrib contrib-type="author"><name><surname>Sali</surname><given-names>Adnan</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">†</xref></contrib><contrib contrib-type="author"><name><surname>Dubljevic</surname><given-names>Valentina</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">†</xref></contrib><contrib contrib-type="author"><name><surname>Lenoir</surname><given-names>Christelle</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">*</xref></contrib><contrib contrib-type="author"><name><surname>Trugnan</surname><given-names>Germain</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">*</xref></contrib><contrib contrib-type="author"><name><surname>Maurice</surname><given-names>Michèle</given-names></name><xref ref-type="aff" rid="N0x9ed5310.0x8bab9b8">*</xref><xref ref-type="author-notes" rid="FN152">‡</xref></contrib></contrib-group><aff id="N0x9ed5310.0x8bab9b8"><label>*</label>U538 INSERM, CHU St-Antoine, 75571 Paris Cedex 12, France; and<label>†</label>Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia</aff><contrib-group><contrib contrib-type="editor"><name><surname>Guidotti</surname><given-names>Guido</given-names></name><role>Monitoring Editor</role></contrib></contrib-group><author-notes><fn id="FN152"><label>‡</label><p>Corresponding author. E-mail address: <email>maurice@st-antoine.inserm.fr</email></p></fn></author-notes><pub-date pub-type="ppub"><month>10</month><year>2001</year></pub-date><volume>12</volume><issue>10</issue><fpage>3004</fpage><lpage>3015</lpage><history><date date-type="received"><day>3</day><month>1</month><year>2001</year></date><date date-type="rev-recd"><day>24</day><month>5</month><year>2001</year></date><date date-type="accepted"><day>19</day><month>7</month><year>2001</year></date></history><copyright-statement>Copyright © 2001, The American Society for Cell Biology</copyright-statement><copyright-year>2001</copyright-year><abstract><p>Enzymes of the nucleotide pyrophosphatase/phosphodiesterase (NPPase) family are expressed at opposite surfaces in polarized epithelial cells. We investigated the targeting signal of NPP1, which is exclusively expressed at the basolateral surface. Full-length NPP1 and different constructs and mutants were transfected into the polarized MDCK cell line. Expression of the proteins was analyzed by confocal microscopy and surface biotinylation. The basolateral signal of NPP1 was identified as a di-leucine motif located in the cytoplasmic tail. Mutation of either or both leucines largely redirected NPP1 to the apical surface. Furthermore, addition of the conserved sequence AAASLLAP redirected the apical nucleotide pyrophosphatase/phosphodiesterase NPP3 to the basolateral surface. Full-length NPP1 was not significantly internalized. However, when the cytoplasmic tail was deleted upstream the di-leucine motif or when the six upstream flanking amino acids were deleted, the protein was mainly found intracellularly. Endocytosis experiments indicated that these mutants were endocytosed from the basolateral surface. These results identify the basolateral signal of NPP1 as a short sequence including a di-leucine motif that is dominant over apical determinants and point to the importance of surrounding amino acids in determining whether the signal will function as a basolateral signal only or as an endocytotic signal as well.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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