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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">GLUT-4</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_2.A.1.1" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">

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<th colspan="3" style="background:#90EE90; color:#202122;">GLUT-4
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<td colspan="3"><span typeof="mw:File"></span>
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<th colspan="3" style="background:#90EE90; color:#202122;;">Eigenschaften des menschlichen Proteins
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<td><a href="Molare_Masse" title="Molare Masse">Masse</a>/Länge <a href="Prim%C3%A4rstruktur" title="Primärstruktur">Primärstruktur</a>
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<td colspan="2" style="text-align:center;">509 Aminosäuren
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<td><a href="Sekund%C3%A4rstruktur" title="Sekundärstruktur">Sekundär-</a> bis <a href="Quart%C3%A4rstruktur" title="Quartärstruktur">Quartärstruktur</a>
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<td colspan="2" style="text-align:center;">multipass (12 TMS) Membranprotein
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td><a href="Human_Genome_Organisation" title="Human Genome Organisation">Gen-Name</a>
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<td colspan="2" class="" style="text-align:center;"><i><a rel="nofollow" class="external text" href="https://www.genenames.org/tools/search/#!/all?query=11109">SLC2A4</a></i>
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<td>Externe IDs
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<td colspan="2" class="">
<ul><li><a href="Online_Mendelian_Inheritance_in_Man" title="Online Mendelian Inheritance in Man">OMIM</a>:&nbsp;<a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/omim/138190">138190</a></li>
<li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P14672">P14672</a></li></ul>
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<th colspan="3" style="background:#90EE90; color:#202122;">Transporter-Klassifikation
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<td><a href="Transporter_Classification_Database" title="Transporter Classification Database">TCDB</a>
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<td colspan="2" class="" style="text-align:center;"><a rel="nofollow" class="external text" href="https://tcdb.org/search/result.php?tc=2.A.1.1">2.A.1.1</a>
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<td><a href="Membrantransport" title="Membrantransport">Bezeichnung</a>
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<td colspan="2" style="text-align:center;"><a href="Major-Facilitator-Superfamilie" title="Major-Facilitator-Superfamilie">Major-Facilitator-Superfamilie</a> / <a href="Glucosetransporter" title="Glucosetransporter">Glucosetransporter</a>
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<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Homologie-Familie
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<td colspan="2" style="text-align:center;"><a rel="nofollow" class="external text" href="http://hogenom.univ-lyon1.fr/query_sequence?seq=P14672">Hovergen</a>
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<td style="background:#C3FDB8; color:#202122;">Übergeordnetes <a href="Taxon" title="Taxon">Taxon</a>
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<td colspan="2" style="text-align:center;"><a href="S%C3%A4ugetiere" title="Säugetiere">Säugetiere</a><sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>
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</p><p><b>GLUT-4 (Glucosetransporter Typ 4)</b> (<a href="Gen" title="Gen">Gen</a>: <i>SLC2A4</i>) ist ein <a href="Protein" title="Protein">Protein</a>, das besonders in <a href="Vesikel_(Biologie)" title="Vesikel (Biologie)">Vesikeln</a> in <a href="S%C3%A4ugetiere" title="Säugetiere">Säugetier</a>-<a href="Zelle_(Biologie)" title="Zelle (Biologie)">Zellen</a> lokalisiert ist. Bei GLUT-4 handelt es sich um ein Membran-<a href="Transportprotein" title="Transportprotein">Transportprotein</a>. Beim Menschen wird GLUT-4 in gestreiften Muskel- und Fettzellen <a href="Genexpression" title="Genexpression">exprimiert</a>. Eine der Konsequenzen des Andockens von <a href="Insulin" title="Insulin">Insulin</a> an den <a href="Insulinrezeptor" title="Insulinrezeptor">Insulinrezeptor</a> ist, dass sich die GLUT-4-Vesikel mit der <a href="Zellmembran" title="Zellmembran">Zellmembran</a> vereinen und somit die Einschleusung von <a href="Glucose" title="Glucose">Glucose</a> in die Zelle angekurbelt wird. <a href="Mutation" title="Mutation">Mutationen</a> im <i>GLUT4</i>-Gen können zu GLUT-4-Mangel und dieser zu einer (seltenen) erblichen Form des <a href="Diabetes_mellitus" title="Diabetes mellitus">Diabetes mellitus</a> Typ&nbsp;2 führen.<sup id="cite_ref-u_2-0" class="reference"><a href="#cite_note-u-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup>
</p>

<div class="mw-heading mw-heading2"><h2 id="Funktion">Funktion</h2></div>
<p>Bei niedrigem Insulinlevel wandern die GLUT-4-Vesikel langsam zu den <a href="Endosom" title="Endosom">Endosomen</a> und werden dort abgebaut. Steigt der Blutzuckerspiegel an, steigt auch der Insulinspiegel. Insulin vermittelt die Fusion der Vesikel mit der Plasmamembran. Nach Umlenkung der Vesikel zur Außenmembran durch Insulin-<a href="Signaltransduktion" title="Signaltransduktion">Signaltransduktion</a> kann die Glucoseaufnahme der Zelle schnell auf den 20- bis 50-fachen Wert steigen. Danach werden die Transporter durch <a href="Endozytose" title="Endozytose">Endozytose</a> wieder aufgenommen und können erneut verwendet werden. In den Fettzellen kann die Glucose dann in <a href="Triacylglycerine" class="mw-redirect" title="Triacylglycerine">Triacylglycerine</a> umgewandelt, in Muskelzellen in Form von <a href="Glykogen" title="Glykogen">Glykogen</a>, gespeichert werden. GLUT-4 hat große Ähnlichkeit mit <a href="GLUT-1" title="GLUT-1">GLUT-1</a>, kann jedoch kein DHA transportieren.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Regulation">Regulation</h2></div>
<p>Die Glucoseaufnahme von Muskelzellen wird über die Anzahl der GLUT-4-Moleküle in der Membran und gleichzeitig die Häufigkeit ihres Recycling mittels Endozytose reguliert. Außerdem kann sich die Aktivität des Transporters verändern. Die Anzahl der GLUT-4-Transporter wird dabei hauptsächlich durch die Wirkungen des Insulins erhöht. Die Recyclingrate kann durch Muskelkontraktion, -depolarisierung oder Energiemangel gebremst werden. Die Aktivität ist erniedrigt, wenn die Enzyme <a href="Glycerinaldehyd-3-phosphat-Dehydrogenase" title="Glycerinaldehyd-3-phosphat-Dehydrogenase">Glycerinaldehyd-3-phosphat-Dehydrogenase</a> oder <a href="Hexokinase" title="Hexokinase">Hexokinase</a>&nbsp;II an GLUT-4 binden.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Weiterführende_Literatur"><span id="Weiterf.C3.BChrende_Literatur"></span>Weiterführende Literatur</h2></div>
<ul><li>Mohan S S, Perry JJ, Poulose N, Nair BG, Anilkumar G: <cite style="font-style:italic">Homology modeling of GLUT4, an insulin regulated facilitated glucose transporter and docking studies with ATP and its inhibitors</cite>. In: <cite style="font-style:italic">J. Biomol. Struct. Dyn.</cite> 26. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em">&nbsp;</span>4</span>, Februar 2009, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em">&nbsp;</span>455–64</span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/19108584?dopt=Abstract">PMID 19108584</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rfr_id=info:sid/de.wikipedia.org:GLUT-4&amp;rft.atitle=Homology+modeling+of+GLUT4%2C+an+insulin+regulated+facilitated+glucose+transporter+and+docking+studies+with+ATP+and+its+inhibitors&amp;rft.au=Mohan+S+S%2C+Perry+JJ%2C+Poulose+N%2C+...&amp;rft.date=2009-02&amp;rft.genre=journal&amp;rft.issue=4&amp;rft.jtitle=J.+Biomol.+Struct.+Dyn.&amp;rft.pages=455-64&amp;rft.pmid=19108584&amp;rft.volume=26.+Jahrgang" style="display:none">&nbsp;</span></li></ul>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="http://omabrowser.org/cgi-bin/gateway.pl?f=DisplayGroup&amp;p1=P14672">Orthologe bei OMA</a></span>
</li>
<li id="cite_note-u-2"><span class="mw-cite-backlink"><a href="#cite_ref-u_2-0">↑</a></span> <span class="reference-text"><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P14672">P14672</a></span>
</li>
<li id="cite_note-3"><span class="mw-cite-backlink"><a href="#cite_ref-3">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="http://www.ebi.ac.uk/interpro/IEntry?ac=IPR002441">InterPro: <i>IPR002441 Glucose transporter, type 4 (GLUT4)</i></a></span>
</li>
<li id="cite_note-4"><span class="mw-cite-backlink"><a href="#cite_ref-4">↑</a></span> <span class="reference-text">Klip A: <cite style="font-style:italic">The many ways to regulate glucose transporter 4</cite>. In: <cite style="font-style:italic">Appl Physiol Nutr Metab</cite>. 34. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em">&nbsp;</span>3</span>, Juni 2009, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em">&nbsp;</span>481–7</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1139/h09-047">10.1139/h09-047</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/19448718?dopt=Abstract">PMID 19448718</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rfr_id=info:sid/de.wikipedia.org:GLUT-4&amp;rft.atitle=The+many+ways+to+regulate+glucose+transporter+4&amp;rft.au=Klip+A&amp;rft.date=2009-06&amp;rft.doi=10.1139%2Fh09-047&amp;rft.genre=journal&amp;rft.issue=3&amp;rft.jtitle=Appl+Physiol+Nutr+Metab&amp;rft.pages=481-7&amp;rft.pmid=19448718&amp;rft.volume=34.+Jahrgang" style="display:none">&nbsp;</span></span>
</li>
<li id="cite_note-5"><span class="mw-cite-backlink"><a href="#cite_ref-5">↑</a></span> <span class="reference-text">Antonescu CN, Foti M, Sauvonnet N, Klip A: <cite style="font-style:italic">Ready, set, internalize: mechanisms and regulation of GLUT4 endocytosis</cite>. In: <cite style="font-style:italic">Biosci. Rep.</cite> 29. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em">&nbsp;</span>1</span>, Februar 2009, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em">&nbsp;</span>1–11</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1042/BSR20080105">10.1042/BSR20080105</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/19143591?dopt=Abstract">PMID 19143591</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rfr_id=info:sid/de.wikipedia.org:GLUT-4&amp;rft.atitle=Ready%2C+set%2C+internalize%3A+mechanisms+and+regulation+of+GLUT4+endocytosis&amp;rft.au=Antonescu+CN%2C+Foti+M%2C+Sauvonnet+N%2C+...&amp;rft.date=2009-02&amp;rft.doi=10.1042%2FBSR20080105&amp;rft.genre=journal&amp;rft.issue=1&amp;rft.jtitle=Biosci.+Rep.&amp;rft.pages=1-11&amp;rft.pmid=19143591&amp;rft.volume=29.+Jahrgang" style="display:none">&nbsp;</span></span>
</li>
<li id="cite_note-6"><span class="mw-cite-backlink"><a href="#cite_ref-6">↑</a></span> <span class="reference-text">Zaid H, Talior-Volodarsky I, Antonescu C, Liu Z, Klip A: <cite style="font-style:italic">GAPDH binds GLUT4 reciprocally to hexokinase-II and regulates glucose transport activity</cite>. In: <cite style="font-style:italic">Biochem. J.</cite> 419. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em">&nbsp;</span>2</span>, April 2009, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em">&nbsp;</span>475–84</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1042/BJ20081319">10.1042/BJ20081319</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/19140804?dopt=Abstract">PMID 19140804</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rfr_id=info:sid/de.wikipedia.org:GLUT-4&amp;rft.atitle=GAPDH+binds+GLUT4+reciprocally+to+hexokinase-II+and+regulates+glucose+transport+activity&amp;rft.au=Zaid+H%2C+Talior-Volodarsky+I%2C+Antonescu+C%2C+...&amp;rft.date=2009-04&amp;rft.doi=10.1042%2FBJ20081319&amp;rft.genre=journal&amp;rft.issue=2&amp;rft.jtitle=Biochem.+J.&amp;rft.pages=475-84&amp;rft.pmid=19140804&amp;rft.volume=419.+Jahrgang" style="display:none">&nbsp;</span></span>
</li>
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