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DLG1
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<h2 id="function">Function</h2> <p>SAP97 is expressed throughout the body in epithelial cells, including the kidney and brain.<a class="footnote-ref" id="fnref:1" href="#fn:1"><sup>1</sup></a> There is some evidence that SAP97 regulates cell-to-cell adhesion during cell death, and may interact with <a href="/facts/HPV/7XW8mjG2">HPV</a>. In the brain, SAP97's function is involved in the trafficking of transmembrane receptors from the ER to the plasma membrane.<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a> </p><p>SAP97's function has been investigated by reducing its expression by <a href="/facts/Gene_knockout/RJTMDbUR">knockout</a> or increasing its expression <a href="/facts/Heterologous/C82vxWU8">heterologously</a>. Mice in which the SAP97 gene has been knocked out die perinatally, have a <a href="/facts/Cleft_palate/CoLE8Wbu">cleft palate</a>, and deficiencies in renal function.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a><a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> <a href="/facts/Overexpression/N9yVF3lR">Overexpression</a> of SAP97 in mammalian neurons leads to increased <a href="/facts/Synapse/vdMRJCUn">synaptic</a> strength.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <p>Mutations in DLG1 are associated to <a href="/facts/Crohn%2527s_disease/zm55cBtd">Crohn's disease</a>.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p> <h2 id="structure">Structure</h2> <p>SAP97's protein structure consists of an alternatively-spliced N-terminal domain, three <a href="/facts/PDZ_domain/kSanExq4">PDZ domains</a>, an <a href="/facts/SH3_domain/aFNwnKe8">SH3 domain</a>, hook domain, I3 domain, and finally an inactive <a href="/facts/Guanylate_kinase/hka0h72n">guanylate kinase</a> (GK) domain. Each of these domains has specific interacting partners that help define SAP97's unique function. </p><p>The N-terminal of SAP97 can be alternatively spliced to contain a double-cysteine/palmitoylation site (α-isoform), or an L27 domain (β-isoform. The L27 domain is involved in SAP97 <a href="/facts/Oligomerization/v7oDY8zu">oligomerization</a> with other SAP97 molecules, CASK, and other L27-domain-containing proteins.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> There is also a <a href="/facts/Myosin/7zGeRkpS">myosin</a> VI binding site near N-terminal which may be involved in the internalization of AMPAR.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> </p><p>Each of SAP97's PDZ domains have different binding partners, including the AMPAR subunit GluR1<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a><a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> for the first PDZ domain, and <a href="/facts/Neuroligin/szDHAzcd">neuroligin</a> for the last. SAP97's I3 domain is unique to SAP97 among the MAGUK family, and is known to regulate the post-synaptic localization of SAP97<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> and to bind the protein 4.1N. The GK domain allows SAP97 to bind to <a href="/facts/Gkap/YVtyelbB">GKAP</a>/SAPAP-family proteins. </p> <h2 id="further-reading">Further reading</h2> <ul><li>Humbert P, Russell S, Richardson H (Jun 2003). "Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer". <i>BioEssays</i>. 25 (6): 542–53. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fbies.10286">10.1002/bies.10286</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12766944">12766944</a>.</li> <li>Mukherjee A, Varma SK, Natarajan K (Feb 1972). "Ankle joint instability in poliomyelitis". <i>Indian Journal of Pediatrics</i>. 39 (289): 37–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1007%2FBF02799404">10.1007/BF02799404</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/5024025">5024025</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:46659798">46659798</a>.</li> <li>Kim E, Niethammer M, Rothschild A, Jan YN, Sheng M (Nov 1995). "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases". <i>Nature</i>. 378 (6552): 85–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1995Natur.378...85K">1995Natur.378...85K</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F378085a0">10.1038/378085a0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7477295">7477295</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4362906">4362906</a>.</li> <li><a href="/facts/Robert_Lue/kFMBXEXW">Lue RA</a>, Marfatia SM, <a href="/facts/Daniel_Branton/ByR2FX7T">Branton D</a>, Chishti AH (Oct 1994). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC44908">"Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 91 (21): 9818–22. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1994PNAS...91.9818L">1994PNAS...91.9818L</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.91.21.9818">10.1073/pnas.91.21.9818</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC44908">44908</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7937897">7937897</a>.</li> <li>Niethammer M, Kim E, Sheng M (Apr 1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578538">"Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases"</a>. <i>The Journal of Neuroscience</i>. 16 (7): 2157–63. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1523%2FJNEUROSCI.16-07-02157.1996">10.1523/JNEUROSCI.16-07-02157.1996</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578538">6578538</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8601796">8601796</a>.</li> <li>Azim AC, Knoll JH, Marfatia SM, Peel DJ, Bryant PJ, Chishti AH (Dec 1995). "DLG1: chromosome location of the closest human homologue of the Drosophila discs large tumor suppressor gene". <i>Genomics</i>. 30 (3): 613–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fgeno.1995.1286">10.1006/geno.1995.1286</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8825652">8825652</a>.</li> <li>Lue RA, Brandin E, Chan EP, Branton D (Nov 1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133382">"Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain"</a>. <i>The Journal of Cell Biology</i>. 135 (4): 1125–37. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.135.4.1125">10.1083/jcb.135.4.1125</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133382">2133382</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8922391">8922391</a>.</li> <li>Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y (May 1997). <a href="https://doi.org/10.1074%2Fjbc.272.18.11943">"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density"</a>. <i>The Journal of Biological Chemistry</i>. 272 (18): 11943–51. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.18.11943">10.1074/jbc.272.18.11943</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9115257">9115257</a>.</li> <li>Horio Y, Hibino H, Inanobe A, Yamada M, Ishii M, Tada Y, Satoh E, Hata Y, Takai Y, Kurachi Y (May 1997). <a href="https://doi.org/10.1074%2Fjbc.272.20.12885">"Clustering and enhanced activity of an inwardly rectifying potassium channel, Kir4.1, by an anchoring protein, PSD-95/SAP90"</a>. <i>The Journal of Biological Chemistry</i>. 272 (20): 12885–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.20.12885">10.1074/jbc.272.20.12885</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9148889">9148889</a>.</li> <li>Lee SS, Weiss RS, Javier RT (Jun 1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21216">"Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 94 (13): 6670–5. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1997PNAS...94.6670L">1997PNAS...94.6670L</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.94.13.6670">10.1073/pnas.94.13.6670</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21216">21216</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9192623">9192623</a>.</li> <li>Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (Jun 1997). <a href="https://doi.org/10.1046%2Fj.1365-2443.1997.1310329.x">"DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95"</a>. <i>Genes to Cells</i>. 2 (6): 415–24. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1046%2Fj.1365-2443.1997.1310329.x">10.1046/j.1365-2443.1997.1310329.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9286858">9286858</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:8934092">8934092</a>.</li> <li>Hanada T, Lin L, Chandy KG, Oh SS, Chishti AH (Oct 1997). <a href="https://doi.org/10.1074%2Fjbc.272.43.26899">"Human homologue of the Drosophila discs large tumor suppressor binds to p56lck tyrosine kinase and Shaker type Kv1.3 potassium channel in T lymphocytes"</a>. <i>The Journal of Biological Chemistry</i>. 272 (43): 26899–904. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.43.26899">10.1074/jbc.272.43.26899</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9341123">9341123</a>.</li> <li>Reuver SM, Garner CC (Apr 1998). "E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton". <i>Journal of Cell Science</i>. 111 (8): 1071–80. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1242%2Fjcs.111.8.1071">10.1242/jcs.111.8.1071</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9512503">9512503</a>.</li> <li>Leonard AS, Davare MA, Horne MC, Garner CC, Hell JW (Jul 1998). <a href="https://doi.org/10.1074%2Fjbc.273.31.19518">"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit"</a>. <i>The Journal of Biological Chemistry</i>. 273 (31): 19518–24. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.31.19518">10.1074/jbc.273.31.19518</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9677374">9677374</a>.</li> <li>Deguchi M, Hata Y, Takeuchi M, Ide N, Hirao K, Yao I, Irie M, Toyoda A, Takai Y (Oct 1998). <a href="https://doi.org/10.1074%2Fjbc.273.41.26269">"BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein"</a>. <i>The Journal of Biological Chemistry</i>. 273 (41): 26269–72. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.41.26269">10.1074/jbc.273.41.26269</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9756850">9756850</a>.</li> <li>Brenman JE, Topinka JR, Cooper EC, McGee AW, Rosen J, Milroy T, Ralston HJ, Bredt DS (Nov 1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793550">"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A"</a>. <i>The Journal of Neuroscience</i>. 18 (21): 8805–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1523%2FJNEUROSCI.18-21-08805.1998">10.1523/JNEUROSCI.18-21-08805.1998</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793550">6793550</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9786987">9786987</a>.</li> <li>Bassand P, Bernard A, Rafiki A, Gayet D, Khrestchatisky M (Jun 1999). "Differential interaction of the tSXV motifs of the NR1 and NR2A NMDA receptor subunits with PSD-95 and SAP97". <i>The European Journal of Neuroscience</i>. 11 (6): 2031–43. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1046%2Fj.1460-9568.1999.00611.x">10.1046/j.1460-9568.1999.00611.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10336672">10336672</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:25611356">25611356</a>.</li> <li>Firestein BL, Firestein BL, Brenman JE, Aoki C, Sanchez-Perez AM, El-Husseini AE, Bredt DS (Nov 1999). <a href="https://doi.org/10.1016%2FS0896-6273%2800%2981120-4">"Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting"</a>. <i>Neuron</i>. 24 (3): 659–72. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0896-6273%2800%2981120-4">10.1016/S0896-6273(00)81120-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10595517">10595517</a>.</li> <li>Hibino H, Inanobe A, Tanemoto M, Fujita A, Doi K, Kubo T, Hata Y, Takai Y, Kurachi Y (Jan 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171779">"Anchoring proteins confer G protein sensitivity to an inward-rectifier K(+) channel through the GK domain"</a>. <i>The EMBO Journal</i>. 19 (1): 78–83. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F19.1.78">10.1093/emboj/19.1.78</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171779">1171779</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10619846">10619846</a>.</li> <li>Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL (Jan 2000). "Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding". <i>Cancer Research</i>. 60 (1): 35–7. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10646847">10646847</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="http://www.sdbonline.org/fly/newgene/disclrg1.htm"><i>Drosophila</i> <i>discs large 1</i> - The Interactive Fly</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Müller BM, Kistner U, Veh RW, Cases-Langhoff C, Becker B, Gundelfinger ED, Garner CC (Mar 1995). "Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein". The Journal of Neuroscience. 15 (3 Pt 2): 2354–66. doi:10.1523/JNEUROSCI.15-03-02354.1995. PMC 6578138. PMID 7891172. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578138" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6578138</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Sans N, Racca C, Petralia RS, Wang YX, McCallum J, Wenthold RJ (Oct 2001). "Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway". The Journal of Neuroscience. 21 (19): 7506–16. doi:10.1523/JNEUROSCI.21-19-07506.2001. PMC 6762903. PMID 11567040. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6762903" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6762903</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Caruana G, Bernstein A (Mar 2001). "Craniofacial dysmorphogenesis including cleft palate in mice with an insertional mutation in the discs large gene". Molecular and Cellular Biology. 21 (5): 1475–83. doi:10.1128/MCB.21.5.1475-1483.2001. PMC 86693. PMID 11238884. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86693" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86693</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Mahoney ZX, Sammut B, Xavier RJ, Cunningham J, Go G, Brim KL, Stappenbeck TS, Miner JH, Swat W (Dec 2006). "Discs-large homolog 1 regulates smooth muscle orientation in the mouse ureter". Proceedings of the National Academy of Sciences of the United States of America. 103 (52): 19872–7. Bibcode:2006PNAS..10319872M. doi:10.1073/pnas.0609326103. PMC 1750896. PMID 17172448. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1750896" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1750896</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Rumbaugh G, Sia GM, Garner CC, Huganir RL (Jun 2003). "Synapse-associated protein-97 isoform-specific regulation of surface AMPA receptors and synaptic function in cultured neurons". The Journal of Neuroscience. 23 (11): 4567–76. doi:10.1523/JNEUROSCI.23-11-04567.2003. PMC 6740810. PMID 12805297. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6740810" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6740810</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Xu S, Zhou F, Tao J, Song L, Ng SC, Wang X, Chen L, Yi F, Ran Z, Zhou R, Xia B (2014). "Exome sequencing identifies DLG1 as a novel gene for potential susceptibility to Crohn's disease in a Chinese family study". PLOS ONE. 9 (6): e99807. Bibcode:2014PLoSO...999807X. doi:10.1371/journal.pone.0099807. PMC 4061034. 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The Journal of Biological Chemistry. 277 (34): 30928–34. doi:10.1074/jbc.M203735200. PMID 12050163. <a href="https://doi.org/10.1074%2Fjbc.M203735200" target="_blank">https://doi.org/10.1074%2Fjbc.M203735200</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Osterweil E, Wells DG, Mooseker MS (Jan 2005). "A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis". The Journal of Cell Biology. 168 (2): 329–38. doi:10.1083/jcb.200410091. PMC 2171578. PMID 15657400. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171578" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171578</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Leonard AS, Davare MA, Horne MC, Garner CC, Hell JW (Jul 1998). "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit". The Journal of Biological Chemistry. 273 (31): 19518–24. doi:10.1074/jbc.273.31.19518. 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