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            <title xml:lang="en">The polycystin-1, lipoxygenase, and α -toxin domain regulates polycystin-1 trafficking</title>
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                <forename type="first">Albert C.M.</forename>
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            <idno type="halRefHtml">&lt;i&gt;Journal of the American Society of Nephrology&lt;/i&gt;, 2016, 27 (4), pp.1159-1173. &lt;a target="_blank" href="https://dx.doi.org/10.1681/ASN.2014111074"&gt;&amp;#x27E8;10.1681/ASN.2014111074&amp;#x27E9;&lt;/a&gt;</idno>
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                <title xml:lang="en">The polycystin-1, lipoxygenase, and α -toxin domain regulates polycystin-1 trafficking</title>
                <author role="aut">
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                    <forename type="first">Yaoxian</forename>
                    <surname>Xu</surname>
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                <author role="aut">
                  <persName>
                    <forename type="first">Andrew</forename>
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                <author role="aut">
                  <persName>
                    <forename type="first">Andrea</forename>
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                  <persName>
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                  <persName>
                    <forename type="first">Frédéric</forename>
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                    <forename type="first">Andrew</forename>
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                <author role="aut">
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                    <forename type="first">Jean-Pierre</forename>
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                  <persName>
                    <forename type="first">Oliver</forename>
                    <surname>Wessely</surname>
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                  <idno type="halauthorid">2135101-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">Michael</forename>
                    <surname>Williamson</surname>
                  </persName>
                  <idno type="halauthorid">1571638-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">Albert C.M.</forename>
                    <surname>Ong</surname>
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                <idno type="issn">1046-6673</idno>
                <idno type="eissn">1533-3450</idno>
                <title level="j">Journal of the American Society of Nephrology</title>
                <imprint>
                  <publisher>American Society of Nephrology</publisher>
                  <biblScope unit="volume">27</biblScope>
                  <biblScope unit="issue">4</biblScope>
                  <biblScope unit="pp">1159-1173</biblScope>
                  <date type="datePub">2016-03-31</date>
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              <idno type="doi">10.1681/ASN.2014111074</idno>
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              <classCode scheme="halDomain" n="sdv.bbm.bm">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology</classCode>
              <classCode scheme="halDomain" n="sdv.bbm.mn">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular Networks [q-bio.MN]</classCode>
              <classCode scheme="halDomain" n="sdv.bc.ic">Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]</classCode>
              <classCode scheme="halDomain" n="sdv.bdlr.rs">Life Sciences [q-bio]/Reproductive Biology/Sexual reproduction</classCode>
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              <p>Mutations in polycystin-1 (PC1) give rise to autosomal dominant polycystic kidney disease, an important and common cause of kidney failure. Despite its medical importance, the function of PC1 remains poorly understood. Here, we investigated the role of the intracellular polycystin-1, lipoxygenase, and alpha-toxin (PLAT) signature domain of PC1 using nuclear magnetic resonance, biochemical, cellular, and in vivo functional approaches. We found that the PLAT domain targets PC1 to the plasma membrane in polarized epithelial cells by a mechanism involving the selective binding of the PLAT domain to phosphatidylserine and L-alpha-phosphatidylinositol-4-phosphate (PI4P) enriched in the plasma membrane. This process is regulated by protein kinase A phosphorylation of the PLAT domain, which reduces PI4P binding and recruits beta-arrestins and the clathrin adaptor AP2 to trigger PC1 internalization. Our results reveal a physiological role for the PC1-PLAT domain in renal epithelial cells and suggest that phosphorylation-dependent internalization of PC1 is closely linked to its function in renal development and homeostasis.</p>
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