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            <title xml:lang="en">The Association of Shiga-like Toxin with Detergent-resistant Membranes Is Modulated by Glucosylceramide and Is an Essential Requirement in the Endoplasmic Reticulum for a Cytotoxic Effect</title>
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                <forename type="first">Daniel</forename>
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                <forename type="first">Daniel</forename>
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            <idno type="halRefHtml">&lt;i&gt;Molecular Biology of the Cell&lt;/i&gt;, 2006, 17 (3), pp.1375 - 1387. &lt;a target="_blank" href="https://dx.doi.org/10.1091/mbc.e05-11-1035"&gt;&amp;#x27E8;10.1091/mbc.e05-11-1035&amp;#x27E9;&lt;/a&gt;</idno>
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            <idno type="stamp" n="INSERM">INSERM - Institut national de la santé et de la recherche médicale</idno>
            <idno type="stamp" n="UPMC" corresp="SORBONNE-UNIVERSITE">Université Pierre et Marie Curie</idno>
            <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
            <idno type="stamp" n="FNCLCC" corresp="INSERM">UNICANCER</idno>
            <idno type="stamp" n="CURIE" corresp="INSERM">Institut Curie</idno>
            <idno type="stamp" n="UMR144" corresp="SORBONNE-UNIVERSITE">Biologie cellulaire et cancer</idno>
            <idno type="stamp" n="PSL">Université Paris sciences et lettres</idno>
            <idno type="stamp" n="UPMC_POLE_4" corresp="UPMC">UPMC Pôle 4</idno>
            <idno type="stamp" n="SORBONNE-UNIVERSITE">Sorbonne Université</idno>
            <idno type="stamp" n="SU-SCIENCES" corresp="SORBONNE-UNIVERSITE">Faculté des Sciences de Sorbonne Université</idno>
            <idno type="stamp" n="INSTITUT-CURIE-PSL" corresp="PSL">Institut Curie - PSL</idno>
            <idno type="stamp" n="SU-TI">Sorbonne Université - Texte Intégral</idno>
            <idno type="stamp" n="ALLIANCE-SU"> Alliance Sorbonne Université</idno>
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                <title xml:lang="en">The Association of Shiga-like Toxin with Detergent-resistant Membranes Is Modulated by Glucosylceramide and Is an Essential Requirement in the Endoplasmic Reticulum for a Cytotoxic Effect</title>
                <author role="aut">
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                    <forename type="first">Daniel</forename>
                    <forename type="middle">C</forename>
                    <surname>Smith</surname>
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                    <forename type="first">Daniel</forename>
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                    <surname>Sillence</surname>
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                  <idno type="halauthorid">4084274-0</idno>
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                    <forename type="first">Rosemary</forename>
                    <forename type="middle">M</forename>
                    <surname>Jarvis</surname>
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                <author role="aut">
                  <persName>
                    <forename type="first">Ludger</forename>
                    <surname>Johannes</surname>
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                <author role="aut">
                  <persName>
                    <forename type="first">J. Michael</forename>
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                  <persName>
                    <forename type="first">Frances</forename>
                    <forename type="middle">M</forename>
                    <surname>Platt</surname>
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                  <idno type="halauthorid">4084276-0</idno>
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                    <forename type="first">Lynne</forename>
                    <forename type="middle">M</forename>
                    <surname>Roberts</surname>
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                <title level="j">Molecular Biology of the Cell</title>
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                  <publisher>American Society for Cell Biology</publisher>
                  <biblScope unit="volume">17</biblScope>
                  <biblScope unit="issue">3</biblScope>
                  <biblScope unit="pp">1375 - 1387</biblScope>
                  <date type="datePub">2006-03</date>
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              <idno type="doi">10.1091/mbc.e05-11-1035</idno>
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              <p>Receptor-mediated internalization to the endoplasmic reticulum (ER) and subsequent retro-translocation to the cytosol are essential sequential processes required for the productive intoxication of susceptible mammalian cells by Shiga-like toxin-1 (SLTx). Recently, it has been proposed that the observed association of certain ER-directed toxins and viruses with detergent-resistant membranes (DRM) may provide a general mechanism for their retrograde transport to endoplasmic reticulum (ER). Here, we show that DRM recruitment of SLTx bound to its globotriosylceramide (Gb(3)) receptor is mediated by the availability of other glycosphingolipids. Reduction in glucosylceramide (GlcCer) levels led to complete protection against SLTx and a reduced cell surface association of bound toxin with DRM. This reduction still allowed efficient binding and transport of the toxin to the ER. However, toxin sequestration within DRM of the ER was abolished under reduced GlcCer conditions, suggesting that an association of toxin with lipid microdomains or rafts in the ER (where these are defined by detergent insolubility) is essential for a later step leading to or involving retro-translocation of SLTx across the ER membrane. In support of this, we show that a number of ER residents, proteins intimately involved in the process of ER dislocation of misfolded proteins, are present in DRM.</p>
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