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DLG4
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<h2 id="maguk-superfamily-and-constituent-domains">MAGUK superfamily and constituent domains</h2> <p>PSD-95 (encoded by DLG4) is a member of the MAGUK superfamily, and part of a subfamily which also includes <a href="/facts/DLG2/Ap0FIEGD">PSD-93</a>, <a href="/facts/DLG1/BMBHNeUq">SAP97</a> and <a href="/facts/DLG3/Iz8MeFY6">SAP102</a>. The MAGUKs are defined by their inclusion of <a href="/facts/PDZ_domain/kSanExq4">PDZ</a>, <a href="/facts/SH3_domain/aFNwnKe8">SH3</a> and <a href="/facts/Guanylate_kinase/hka0h72n">GUK</a> domains, although many of them also contain regions homologous of <a href="/facts/Ca2%2B/calmodulin-dependent_protein_kinase/P8xWo0vB">CaMKII</a>, <a href="/facts/WW_domain/se8s4D5V">WW</a> and <a href="/facts/L27_domain/A7RSwS7b">L27</a> domains.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> The GUK domain that they have is structurally very similar to that of the <a href="/facts/Guanylate_kinase/hka0h72n">guanylate kinases</a>, however it is known to be catalytically inactive as the P-Loop which binds <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction. </p><p>The <a href="/facts/PDZ_domain/kSanExq4">PDZ domain</a> which are contained in the MAGUKs in varying numbers, is replicated three times over in PSD-95. PDZ domains are short peptide binding sequences commonly found at the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a> of interacting proteins. The three copies within the gene have different binding partners, due to amino acid substitutions within the PSD-95 protein and its ligands. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state. The regulatory mechanisms and function are unknown but it is hypothesized that it may involve a hook region and a <a href="/facts/Calmodulin/CbEnEYHE">calmodulin</a> binding region located elsewhere in the gene. </p> <h2 id="interactions">Interactions</h2> <p>PSD-95 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/ADAM22/m2bvS2zb">ADAM22</a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a></li> <li><a href="/facts/Beta-1_adrenergic_receptor/mKQVE8tB">Beta-1 adrenergic receptor</a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a></li> <li><a href="/facts/CACNG2/bb2RKzF4">CACNG2</a><a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a></li> <li><a href="/facts/CASK/wJa81fI3">CASK</a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a></li> <li><a href="/facts/DLG3/Iz8MeFY6">DLG3</a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a></li> <li><a href="/facts/DLGAP1/YVtyelbB">DLGAP1</a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a><a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a><a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a><a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a></li> <li><a href="/facts/DLGAP2/Qx341SKm">DLGAP2</a><a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a></li> <li><a href="/facts/DYNLL1/FSvlrBND">DYNLL1</a><a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a></li> <li><a href="/facts/DYNLL2/alIRYsV2">DYNLL2</a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a></li> <li><a href="/facts/ERBB4/7DJ8B0xn">ERBB4</a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a><a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a></li> <li><a href="/facts/EXOC4/8JsKleN1">EXOC4</a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a><a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a></li> <li><a href="/facts/FYN/qCAEbIAb">FYN</a><a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a><a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a></li> <li><a href="/facts/FZD7/dbnTrLFY">FZD7</a><a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a></li> <li><a href="/facts/GRIK1/suqW7gx2">GRIK1</a><a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a></li> <li><a href="/facts/GRIK2/Xw07x5xl">GRIK2</a><a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a><a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a></li> <li><a href="/facts/GRIK5/rJ4RPcU9">GRIK5</a><a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a><a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a></li> <li><a href="/facts/GRIN2A/KE9KrAEj">GRIN2A</a><a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a><a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a><a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a><a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a></li> <li><a href="/facts/GRIN2B/GllS9Fpu">GRIN2B</a><a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a><a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a><a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a><a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a><a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a><a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a></li> <li><a href="/facts/GRIN2C/J4f62bfV">GRIN2C</a><a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a></li> <li><a href="/facts/HER2/neu/xue3SgcA">HER2/neu</a><a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a></li> <li><a href="/facts/HGS_(gene)/E3J4EKkS">HGS</a><a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a></li> <li><a href="/facts/KCNA2/gdzJClLg">KCNA2</a><a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a></li> <li><a href="/facts/KCNA4/WfUl2g4q">KCNA4</a><a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a><a class="footnote-ref" id="fnref:51" href="#fn:51"><sup>51</sup></a><a class="footnote-ref" id="fnref:52" href="#fn:52"><sup>52</sup></a><a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a></li> <li><a href="/facts/KCNA5/kdkkkRy6">KCNA5</a><a class="footnote-ref" id="fnref:54" href="#fn:54"><sup>54</sup></a><a class="footnote-ref" id="fnref:55" href="#fn:55"><sup>55</sup></a></li> <li><a href="/facts/KCNJ12/F0SBwP8d">KCNJ12</a><a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a><a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a><a class="footnote-ref" id="fnref:58" href="#fn:58"><sup>58</sup></a><a class="footnote-ref" id="fnref:59" href="#fn:59"><sup>59</sup></a></li> <li><a href="/facts/Kir2.1/3hDjj7Yt">Kir2.1</a><a class="footnote-ref" id="fnref:60" href="#fn:60"><sup>60</sup></a></li> <li><a href="/facts/LGI1/bNqmIVBR">LGI1</a><a class="footnote-ref" id="fnref:61" href="#fn:61"><sup>61</sup></a></li> <li><a href="/facts/LRP1/0XmdyNpG">LRP1</a><a class="footnote-ref" id="fnref:62" href="#fn:62"><sup>62</sup></a></li> <li><a href="/facts/LRP2/dxfbGQGm">LRP2</a><a class="footnote-ref" id="fnref:63" href="#fn:63"><sup>63</sup></a><a class="footnote-ref" id="fnref:64" href="#fn:64"><sup>64</sup></a></li> <li><a href="/facts/NLGN1/rurbNWKY">NLGN1</a><a class="footnote-ref" id="fnref:65" href="#fn:65"><sup>65</sup></a></li> <li><a href="/facts/NOS1/4KcIMAbM">NOS1</a><a class="footnote-ref" id="fnref:66" href="#fn:66"><sup>66</sup></a><a class="footnote-ref" id="fnref:67" href="#fn:67"><sup>67</sup></a></li> <li><a href="/facts/PTK2B/bESQee1h">PTK2B</a><a class="footnote-ref" id="fnref:68" href="#fn:68"><sup>68</sup></a></li> <li><a href="/facts/SEMA4C/us0z6Tvj">SEMA4C</a><a class="footnote-ref" id="fnref:69" href="#fn:69"><sup>69</sup></a> and</li> <li><a href="/facts/SHANK2/KftzJw2a">SHANK2</a>.<a class="footnote-ref" id="fnref:70" href="#fn:70"><sup>70</sup></a><a class="footnote-ref" id="fnref:71" href="#fn:71"><sup>71</sup></a></li></ul> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Postsynaptic_density/Bj7l0gVY">Postsynaptic density</a></li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=DLG4+protein%2C+human">DLG4 protein, human</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"Entrez Gene: DLG4 discs, large homolog 4 (Drosophila)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1742" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1742</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Cho KO, Hunt CA, Kennedy MB (Nov 1992). "The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein". Neuron. 9 (5): 929–942. doi:10.1016/0896-6273(92)90245-9. PMID 1419001. S2CID 28528759. <a href="/wiki/Mary_B._Kennedy" target="_blank">/wiki/Mary_B._Kennedy</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Stathakis DG, Hoover KB, You Z, Bryant PJ (Nov 1997). "Human postsynaptic density-95 (PSD95): location of the gene (DLG4) and possible function in nonneural as well as in neural tissues". Genomics. 44 (1): 71–82. doi:10.1006/geno.1997.4848. PMID 9286702. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"Entrez Gene: DLG4 discs, large homolog 4 (Drosophila)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1742" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1742</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Hunt CA, Schenker LJ, Kennedy MB (Feb 1996). "PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses". Journal of Neuroscience. 16 (4): 1380–1388. doi:10.1523/JNEUROSCI.16-04-01380.1996. PMC 6578559. PMID 8778289. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578559" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578559</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Sheng M, Sala C (2001). "PDZ domains and the organization of supramolecular complexes". Annu. Rev. Neurosci. 24: 1–29. doi:10.1146/annurev.neuro.24.1.1. PMID 11283303. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Meyer D, Bonhoeffer T, Scheuss V (2014). "Balance and stability of synaptic structures during synaptic plasticity". Neuron. 82 (2): 430–43. doi:10.1016/j.neuron.2014.02.031. PMID 24742464. <a href="https://doi.org/10.1016%2Fj.neuron.2014.02.031" target="_blank">https://doi.org/10.1016%2Fj.neuron.2014.02.031</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Woods DF, Bryant PJ (December 1993). "ZO-1, DlgA and PSD-95/SAP90: homologous proteins in tight, septate and synaptic cell junctions". Mech. Dev. 44 (2–3): 85–9. doi:10.1016/0925-4773(93)90059-7. PMID 8155583. S2CID 5785380. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Fukata Y, Adesnik H, Iwanaga T, Bredt DS, Nicoll RA, Fukata M (September 2006). "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission". Science. 313 (5794): 1792–5. Bibcode:2006Sci...313.1792F. doi:10.1126/science.1129947. PMID 16990550. S2CID 33024022. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Hu LA, Tang Y, Miller WE, Cong M, Lau AG, Lefkowitz RJ, Hall RA (December 2000). "beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors". J. Biol. Chem. 275 (49): 38659–66. doi:10.1074/jbc.M005938200. PMID 10995758. <a href="https://doi.org/10.1074%2Fjbc.M005938200" target="_blank">https://doi.org/10.1074%2Fjbc.M005938200</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Chen L, Chetkovich DM, Petralia RS, Sweeney NT, Kawasaki Y, Wenthold RJ, Bredt DS, Nicoll RA (2000). "Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms". Nature. 408 (6815): 936–43. Bibcode:2000Natur.408..936C. doi:10.1038/35050030. PMID 11140673. S2CID 4427689. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Choi J, Ko J, Park E, Lee JR, Yoon J, Lim S, Kim E (April 2002). "Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD-95". J. Biol. Chem. 277 (14): 12359–63. doi:10.1074/jbc.M200528200. PMID 11805122. <a href="https://doi.org/10.1074%2Fjbc.M200528200" target="_blank">https://doi.org/10.1074%2Fjbc.M200528200</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Chetkovich DM, Bunn RC, Kuo SH, Kawasaki Y, Kohwi M, Bredt DS (August 2002). "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms". J. Neurosci. 22 (15): 6415–25. doi:10.1523/JNEUROSCI.22-15-06415.2002. PMC 6758133. PMID 12151521. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6758133" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6758133</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Masuko N, Makino K, Kuwahara H, Fukunaga K, Sudo T, Araki N, Yamamoto H, Yamada Y, Miyamoto E, Saya H (February 1999). "Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites". J. Biol. Chem. 274 (9): 5782–90. doi:10.1074/jbc.274.9.5782. PMID 10026200. <a href="https://doi.org/10.1074%2Fjbc.274.9.5782" target="_blank">https://doi.org/10.1074%2Fjbc.274.9.5782</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. 20 (12): 4524–34. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMC 6772433. PMID 10844022. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772433" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6772433</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (May 1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density". J. Biol. Chem. 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. PMID 9115257. <a href="https://doi.org/10.1074%2Fjbc.272.18.11943" target="_blank">https://doi.org/10.1074%2Fjbc.272.18.11943</a> <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Boeckers TM, Winter C, Smalla KH, Kreutz MR, Bockmann J, Seidenbecher C, Garner CC, Gundelfinger ED (October 1999). "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family". Biochem. Biophys. Res. Commun. 264 (1): 247–52. doi:10.1006/bbrc.1999.1489. PMID 10527873. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (June 1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells. 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858. S2CID 8934092. <a href="https://doi.org/10.1046%2Fj.1365-2443.1997.1310329.x" target="_blank">https://doi.org/10.1046%2Fj.1365-2443.1997.1310329.x</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>Wu H, Reissner C, Kuhlendahl S, Coblentz B, Reuver S, Kindler S, Gundelfinger ED, Garner CC (November 2000). "Intramolecular interactions regulate SAP97 binding to GKAP". EMBO J. 19 (21): 5740–51. doi:10.1093/emboj/19.21.5740. PMC 305801. 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