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CARD11
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<h2 id="function">Function</h2> <p>The protein encoded by this gene belongs to the <a href="/facts/Membrane-associated_guanylate_kinase/yno8WVFT">membrane-associated guanylate kinase</a> (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (<a href="/facts/CARD_domain/ySJupuCo">CARD</a>). CARD11 (CARMA1) has a domain structure similar to that of <a href="/facts/CARD10/7QLa8j3p">CARD10</a> (CARMA3) and <a href="/facts/CARD14/D8hrq4Mn">CARD14</a> (CARMA2) as a member of the <a href="/facts/CARD-CC_family/AYDhVkdx">CARD-CC family</a> with a C terminal MAGUK domain (the so-called CARMA proteins). The CARD domain of proteins in the <a href="/facts/CARD-CC_family/AYDhVkdx">CARD-CC family</a> have been shown to specifically interact with <a href="/facts/BCL10/Mcut7JI3">BCL10</a>, a protein known to function as a positive regulator of <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a> activation by recruitment and activation of <a href="/facts/MALT1/Az3QuTrY">MALT1</a>. When overexpressed in cells, this protein family activates NF-κB and induces the <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylation</a> of BCL10.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p><p>CARD11 is critical for <a href="/facts/T_cell/5z6PQ9UN">T cell</a> and <a href="/facts/B_cell/6Y1tgwwp">B cell</a> function and is activated after <a href="/facts/T_cell_receptor/zDqyWyG4">T cell receptor</a> or <a href="/facts/B_cell_receptor/J6qRYYkN">B cell receptor</a> stimulation. After receptor stimulation, CARD11 is phosphorylated by <a href="/facts/PKC-%25CE%25B8/6WSQgAWv">PKC-θ</a> (in T cells) or <a href="/facts/PRKCB1/6wQn8hEy">PKC-β</a> (in B cells). The phosphorylation induces formation of filamentous CARD11 multimers that recruit <a href="/facts/BCL10/Mcut7JI3">BCL10</a> and <a href="/facts/MALT1/Az3QuTrY">MALT1</a>, which in turn activates <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a>. Loss of function mutations in CARD11 cause <a href="/facts/Severe_combined_immunodeficiency/gNfMUSp9">severe combined immunodeficiency</a> (SCID) since the function of cells critical for <a href="/facts/Adaptive_immunity/bc7zT1Jo">adaptive immunity</a> are disrupted. </p> <h2 id="structure">Structure</h2> <p>The structure of CARD11 involves multiple domains that impact the protein's ability to activate <a href="/facts/BCL10/Mcut7JI3">BCL10</a> and <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a> activity. CARD11 has a CARD domain, a serine-threonine rich region, is associated with the N-terminus, which is essential for <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a> signaling activity. The region following the CARD domain is highly coiled. In deleting the CARD domain, all <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a> signaling activity was prevented. The CARD domain on CARD11 interacts with the CARD domain on <a href="/facts/BCL10/Mcut7JI3">BCL10</a> to initiate the signaling pathway.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p><p>On the C-terminus of CARD11 there is the MAGUK domain that is associated with the cell membrane. This domain is often referred to as the inhibitory domain. <a href="/facts/Protein_kinase_C/6WSQgAWv">Protein kinase C</a> activates CARD11 by phosphorylating serine residues within the inhibitory domain.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>CARD11 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/BCL10/Mcut7JI3">BCL10</a>.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> This interaction occurs between the CARD domain on <a href="/facts/BCL10/Mcut7JI3">BCL10</a> and the CARD domain on CARD11, and results in signal propagation and NF-κB activation.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p> <h2 id="external-links">External links</h2> <ul><li>Human <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=CARD11"><i>CARD11</i></a> genome location and <a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=CARD11"><i>CARD11</i></a> gene details page in the <a href="/facts/UCSC_Genome_Browser/kwumPyLb">UCSC Genome Browser</a>.</li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (1996). <a href="https://doi.org/10.1101%2Fgr.6.9.807">"Generation and analysis of 280,000 human expressed sequence tags"</a>. <i>Genome Res</i>. 6 (9): 807–28. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgr.6.9.807">10.1101/gr.6.9.807</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8889549">8889549</a>.</li> <li>Sanger Centre T, Washington University Genome Sequencing Cente T (1998). <a href="https://doi.org/10.1101%2Fgr.8.11.1097">"Toward a complete human genome sequence"</a>. <i>Genome Res</i>. 8 (11): 1097–108. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgr.8.11.1097">10.1101/gr.8.11.1097</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9847074">9847074</a>.</li> <li>Wang L, Guo Y, Huang WJ, Ke X, Poyet JL, Manji GA, Merriam S, Glucksmann MA, DiStefano PS, Alnemri ES, Bertin J (2001). <a href="https://doi.org/10.1074%2Fjbc.M102488200">"Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B"</a>. <i>J. Biol. Chem</i>. 276 (24): 21405–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M102488200">10.1074/jbc.M102488200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11259443">11259443</a>.</li> <li>Wang D, You Y, Case SM, McAllister-Lucas LM, Wang L, DiStefano PS, Nuñez G, Bertin J, Lin X (2002). "A requirement for CARMA1 in TCR-induced NF-kappa B activation". <i>Nat. Immunol</i>. 3 (9): 830–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fni824">10.1038/ni824</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12154356">12154356</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:19250072">19250072</a>.</li> <li>Gaide O, Favier B, Legler DF, Bonnet D, Brissoni B, Valitutti S, Bron C, Tschopp J, Thome M (2002). <a href="http://nbn-resolving.de/urn:nbn:de:bsz:352-2-1mitensdcb5c25">"CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation"</a>. <i>Nat. Immunol</i>. 3 (9): 836–43. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fni830">10.1038/ni830</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12154360">12154360</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:42949809">42949809</a>.</li> <li>Pomerantz JL, Denny EM, Baltimore D (2002). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129028">"CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex"</a>. <i>EMBO J</i>. 21 (19): 5184–94. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2Fcdf505">10.1093/emboj/cdf505</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129028">129028</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12356734">12356734</a>.</li> <li>Wang D, Matsumoto R, You Y, Che T, Lin XY, Gaffen SL, Lin X (2004). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC303359">"CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1"</a>. <i>Mol. Cell. Biol</i>. 24 (1): 164–71. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.24.1.164-171.2003">10.1128/MCB.24.1.164-171.2003</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC303359">303359</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14673152">14673152</a>.</li> <li>Stilo R, Liguoro D, Di Jeso B, Formisano S, Consiglio E, Leonardi A, Vito P (2004). <a href="https://doi.org/10.1074%2Fjbc.M402244200">"Physical and functional interaction of CARMA1 and CARMA3 with Ikappa kinase gamma-NFkappaB essential modulator"</a>. <i>J. Biol. Chem</i>. 279 (33): 34323–31. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M402244200">10.1074/jbc.M402244200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15184390">15184390</a>.</li> <li>Lee KY, D'Acquisto F, Hayden MS, Shim JH, Ghosh S (2005). "PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation". <i>Science</i>. 308 (5718): 114–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2005Sci...308..114L">2005Sci...308..114L</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.1107107">10.1126/science.1107107</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15802604">15802604</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:84389997">84389997</a>.</li> <li>Shinohara H, Yasuda T, Aiba Y, Sanjo H, Hamadate M, Watarai H, Sakurai H, Kurosaki T (2005). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2212994">"PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1"</a>. <i>J. Exp. Med</i>. 202 (10): 1423–31. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1084%2Fjem.20051591">10.1084/jem.20051591</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2212994">2212994</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16301747">16301747</a>.</li> <li>Sommer K, Guo B, Pomerantz JL, Bandaranayake AD, Moreno-García ME, Ovechkina YL, Rawlings DJ (2005). <a href="https://doi.org/10.1016%2Fj.immuni.2005.09.014">"Phosphorylation of the CARMA1 linker controls NF-kappaB activation"</a>. <i>Immunity</i>. 23 (6): 561–74. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.immuni.2005.09.014">10.1016/j.immuni.2005.09.014</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16356855">16356855</a>.</li> <li>Matsumoto R, Wang D, Blonska M, Li H, Kobayashi M, Pappu B, Chen Y, Wang D, Lin X (2005). <a href="https://doi.org/10.1016%2Fj.immuni.2005.10.007">"Phosphorylation of CARMA1 plays a critical role in T Cell receptor-mediated NF-kappaB activation"</a>. <i>Immunity</i>. 23 (6): 575–85. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.immuni.2005.10.007">10.1016/j.immuni.2005.10.007</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16356856">16356856</a>.</li> <li>Narayan P, Holt B, Tosti R, Kane LP (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1430296">"CARMA1 is required for Akt-mediated NF-kappaB activation in T cells"</a>. <i>Mol. Cell. Biol</i>. 26 (6): 2327–36. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.26.6.2327-2336.2006">10.1128/MCB.26.6.2327-2336.2006</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1430296">1430296</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16508008">16508008</a>.</li> <li>Ishiguro K, Avruch J, Landry A, Qin S, Ando T, Goto H, Xavier R (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3204664">"Nore1B regulates TCR signaling via Ras and Carma1"</a>. <i>Cell. Signal</i>. 18 (10): 1647–54. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.cellsig.2006.01.015">10.1016/j.cellsig.2006.01.015</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3204664">3204664</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16520020">16520020</a>.</li> <li>Ishiguro K, Green T, Rapley J, Wachtel H, Giallourakis C, Landry A, Cao Z, Lu N, Takafumi A, Goto H, Daly MJ, Xavier RJ (2006). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1592706">"Ca2+/calmodulin-dependent protein kinase II is a modulator of CARMA1-mediated NF-kappaB activation"</a>. <i>Mol. Cell. Biol</i>. 26 (14): 5497–508. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.02469-05">10.1128/MCB.02469-05</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1592706">1592706</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16809782">16809782</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (Apr 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019. <a href="https://doi.org/10.1074%2Fjbc.M010512200" target="_blank">https://doi.org/10.1074%2Fjbc.M010512200</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Gaide O, Martinon F, Micheau O, Bonnet D, Thome M, Tschopp J (May 2001). "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation". FEBS Lett. 496 (2–3): 121–7. doi:10.1016/S0014-5793(01)02414-0. PMID 11356195. S2CID 22024213. <a href="https://doi.org/10.1016%2FS0014-5793%2801%2902414-0" target="_blank">https://doi.org/10.1016%2FS0014-5793%2801%2902414-0</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: CARD11 caspase recruitment domain family, member 11". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84433" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84433</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (Apr 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019. <a href="https://doi.org/10.1074%2Fjbc.M010512200" target="_blank">https://doi.org/10.1074%2Fjbc.M010512200</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>"Entrez Gene: CARD11 caspase recruitment domain family, member 11". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84433" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84433</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (Apr 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019. <a href="https://doi.org/10.1074%2Fjbc.M010512200" target="_blank">https://doi.org/10.1074%2Fjbc.M010512200</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (Apr 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019. <a href="https://doi.org/10.1074%2Fjbc.M010512200" target="_blank">https://doi.org/10.1074%2Fjbc.M010512200</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Holliday MJ, Witt A, Rodriguez Gama A, Walters B, Arthur C, Halfman R, Rohou A, Dueber E, Fairbrother W (2019). "Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation". Nat Commun. 10 (3070): 3070. Bibcode:2019NatCo..10.3070H. doi:10.1038/s41467-019-10953-z. PMC 6624267. PMID 31296852. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6624267" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6624267</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (April 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019. <a href="https://doi.org/10.1074%2Fjbc.M010512200" target="_blank">https://doi.org/10.1074%2Fjbc.M010512200</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Holliday MJ, Witt A, Rodriguez Gama A, Walters B, Arthur C, Halfman R, Rohou A, Dueber E, Fairbrother W (2019). "Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation". Nat Commun. 10 (3070): 3070. Bibcode:2019NatCo..10.3070H. doi:10.1038/s41467-019-10953-z. PMC 6624267. PMID 31296852. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6624267" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6624267</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> </ol>