GJB6

<h2 id="function">Function</h2>
The <a href="/facts/Connexin/RK87nd90">connexin</a> gene family codes for the protein subunits of gap junction channels that mediate direct diffusion of ions and metabolites between the cytoplasm of adjacent cells. Connexins span the plasma membrane 4 times, with amino- and carboxy-terminal regions facing the cytoplasm. Connexin genes are expressed in a cell type-specific manner with overlapping specificity. The gap junction channels have unique properties depending on the type of connexins constituting the channel.[supplied by OMIM]<a class="footnote-ref" id="fnref:6" href="#fn:6">6</a>
Connexin 30 is prevalent in the two distinct gap junction systems found in the cochlea: the epithelial cell gap junction network, which couple non-sensory epithelial cells, and the connective tissue gap junction network, which couple connective tissue cells. Gap junctions serve the important purpose of recycling potassium ions that pass through hair cells during mechanotransduction back to the <a href="/facts/Endolymph/WwYz8dY7">endolymph</a>.<a class="footnote-ref" id="fnref:7" href="#fn:7">7</a>
Connexin 30 has been found to be co-localized with <a href="/facts/GJB2/fxIqb6zc">connexin 26</a>.<a class="footnote-ref" id="fnref:8" href="#fn:8">8</a> Cx30 and Cx26 have also been found to form heteromeric and heterotypic channels. The biochemical properties and channel permeabilities of these more complex channels differ from homotypic Cx30 or Cx26 channels.<a class="footnote-ref" id="fnref:9" href="#fn:9">9</a> Overexpression of Cx30 in Cx30 null mice restored Cx26 expression and normal gap junction channel functioning and calcium signaling, but it is described that Cx26 expression is altered in Cx30 null mice. The researchers hypothesized that co-regulation of Cx26 and Cx30 is dependent on <a href="/facts/Phospholipase_C/Cuo6V7gU">phospholipase C</a> signaling and the <a href="/facts/NF-%CE%BAB/qcpt5vuQ">NF-κB</a> pathway.<a class="footnote-ref" id="fnref:10" href="#fn:10">10</a>
The <a href="/facts/Cochlea/J2ozV2sP">cochlea</a> contains two cell types, auditory <a href="/facts/Hair_cell/dWUGGF0t">hair cells</a> for mechanotransduction and supporting cells. Gap junction channels are only found between cochlear supporting cells.<a class="footnote-ref" id="fnref:11" href="#fn:11">11</a> While gap junctions in the inner ear are critically involved in potassium recycling to the endolymph, connexin expression in the supporting cells surrounding the <a href="/facts/Organ_of_Corti/MMr8p5Cq">organ of Corti</a> have been found to support epithelial tissue lesion repair following loss of sensory hair cells. An experiment with Cx30 null mice found deficits in lesion closure and repair of the organ of Corti following hair cell loss, suggesting that Cx30 has a role in regulating lesion repair response.<a class="footnote-ref" id="fnref:12" href="#fn:12">12</a>
Astrocytes play a crucial role in synaptic physiology and information processing in the brain. A key characteristic of astrocytes is their expression of Cx30, which influences cognitive processes by shaping synaptic and network activities. This Cx-mediated astroglial network regulates the efficiency of extracellular potassium (K+) and glutamate clearance at synapses,<a class="footnote-ref" id="fnref:13" href="#fn:13">13</a> as well as the long-distance trafficking of energy <a href="/facts/Metabolite/nAyywVtA">metabolites</a> to fuel active synapses.<a class="footnote-ref" id="fnref:14" href="#fn:14">14</a><a class="footnote-ref" id="fnref:15" href="#fn:15">15</a> However, Cxs do not only form gap junction channels with other astrocytes; they can also mediate direct exchange with the extracellular space when forming hemichannels.<a class="footnote-ref" id="fnref:16" href="#fn:16">16</a>
Cx30 protein levels set the size of astrocytic networks, and can be modulated by neuronal activity, indicating a close relationship between astrocytic network size and the activation of underlying neuronal networks. However, this modulation is complex, as it differentially impacts principal cells and interneurons.<a class="footnote-ref" id="fnref:17" href="#fn:17">17</a> Additionally, Cx30 can also act via other mechanisms, such as signaling and protein interactions. Recent research has shown that the increase in Cx30 levels between P10 to P50 controls the closure of the <a href="/facts/Critical_period/zcNJmBkf">critical period</a> in the mouse visual cortex through a signaling pathway that regulates the <a href="/facts/Extracellular_matrix/kaHC5Ez8">extracellular matrix</a> and interneuron maturation.<a class="footnote-ref" id="fnref:18" href="#fn:18">18</a>
In the <a href="/facts/Hippocampus/X7CqbP8X">hippocampus</a>, decreased Cx30 expression reduces the size of astroglial networks, while upregulation of Cx30 increases their size.<a class="footnote-ref" id="fnref:19" href="#fn:19">19</a> In both cases, it decreases spontaneous and evoked synaptic transmission. This effect results from reduced neuronal excitability, leading to alterations in the induction of <a href="/facts/Synaptic_plasticity/rdVFxItN">synaptic plasticity</a> and impairments in learning processes in vivo. Altogether, this suggest that astroglial networks have a physiologically optimized size to appropriately regulate neuronal functions.

<h2 id="clinical-significance">Clinical significance</h2>
<h3>Auditory</h3>
<a href="/facts/GJB2/fxIqb6zc">Connexin 26</a> and connexin 30 are commonly accepted to be the predominant gap junction proteins in the <a href="/facts/Cochlea/J2ozV2sP">cochlea</a>. Genetic knockout experiments in mice has shown that knockout of either <a href="/facts/GJB2/fxIqb6zc">Cx26</a> or Cx30 produces deafness.<a class="footnote-ref" id="fnref:20" href="#fn:20">20</a><a class="footnote-ref" id="fnref:21" href="#fn:21">21</a> However, recent research suggests that Cx30 knockout produces deafness due to subsequent downregulation of <a href="/facts/GJB2/fxIqb6zc">Cx26</a>, and one mouse study found that a Cx30 mutation that preserves half of <a href="/facts/GJB2/fxIqb6zc">Cx26</a> expression found in normal Cx30 mice resulted in unimpaired hearing.<a class="footnote-ref" id="fnref:22" href="#fn:22">22</a> The lessened severity of Cx30 knockout in comparison to Cx26 knockout is supported by a study examining the time course and patterns of <a href="/facts/Hair_cell/dWUGGF0t">hair cell</a> degeneration in the cochlea. Cx26 null mice displayed more rapid and widespread cell death than Cx30 null mice. The percent hair cell loss was less widespread and frequent in the cochleas of Cx30 null mice.<a class="footnote-ref" id="fnref:23" href="#fn:23">23</a>

<h3>Sleep cycle</h3>
Connexin 30 (Cx30) appears to play a crucial role in regulating sleep and wakefulness, potentially through its involvement in circadian rhythm generation, response to sleep pressure, and modulation of astrocyte morphology and function.<a class="footnote-ref" id="fnref:24" href="#fn:24">24</a><a class="footnote-ref" id="fnref:25" href="#fn:25">25</a><a class="footnote-ref" id="fnref:26" href="#fn:26">26</a>
Research has shown that Cx30 and Connexin 43 (Cx43) exhibit a time-of-day dependent expression in the mouse suprachiasmatic nucleus (SCN), the central circadian rhythm generator. These connexins contribute to the electric coupling of SCN neurons and astrocytic-neuronal signaling that regulates rhythmic SCN neuronal activity.<a class="footnote-ref" id="fnref:27" href="#fn:27">27</a><a class="footnote-ref" id="fnref:28" href="#fn:28">28</a><a class="footnote-ref" id="fnref:29" href="#fn:29">29</a>
Interestingly, the fluctuation of Cx30 protein expression strongly depends on the light-dark cycle, which suggests that Cx30 may play a role in the circadian system's light entrainment and circadian rhythm generation.<a class="footnote-ref" id="fnref:30" href="#fn:30">30</a><a class="footnote-ref" id="fnref:31" href="#fn:31">31</a><a class="footnote-ref" id="fnref:32" href="#fn:32">32</a>
In a study using Cx30 knockout mice, researchers have found that these mice exhibited a deficit in maintaining wakefulness during periods of high sleep pressure. They needed more stimuli to stay awake during gentle sleep deprivation and showed increased slow-wave sleep during instrumental sleep deprivation.<a class="footnote-ref" id="fnref:33" href="#fn:33">33</a><a class="footnote-ref" id="fnref:34" href="#fn:34">34</a><a class="footnote-ref" id="fnref:35" href="#fn:35">35</a>
Moreover, neuronal activity has been found to increase hippocampal Cx30 protein levels via a posttranslational mechanism regulating lysosomal degradation, which translated at the functional level in the activation of Cx30 hemichannels and in Cx30-mediated remodeling of astrocyte morphology independently of gap junction biochemical coupling.<a class="footnote-ref" id="fnref:36" href="#fn:36">36</a><a class="footnote-ref" id="fnref:37" href="#fn:37">37</a><a class="footnote-ref" id="fnref:38" href="#fn:38">38</a>
The clinical significance of this finding is that it can explain the mechanism of action of <a href="/facts/Modafinil/u8xDYgDU">modafinil</a> in its wakefulness-promoting properties.<a class="footnote-ref" id="fnref:39" href="#fn:39">39</a> Modafinil may promote wakefulness by modulating the function of astroglial connexins, specifically <a href="/facts/Connexin_30/j48d3Ppd">connexin 30</a>, which are proteins that facilitate intercellular communication and play a role in sleep-wake regulation.<a class="footnote-ref" id="fnref:40" href="#fn:40">40</a><a class="footnote-ref" id="fnref:41" href="#fn:41">41</a><a class="footnote-ref" id="fnref:42" href="#fn:42">42</a> Connexins form channels that allow the exchange of ions and signaling molecules between cells. In the brain, they are mainly expressed by astrocytes, which help regulate neuronal activity.<a class="footnote-ref" id="fnref:43" href="#fn:43">43</a> Modafinil increases the levels of connexin 30 in the cortex, enhancing communication between astrocytes and promoting wakefulness. Conversely, connexin 30 levels decrease during sleep, contributing to the transition from wakefulness to sleep. <a href="/facts/Flecainide/pWLJo9zH">Flecainide</a>, a drug that blocks astroglial connexins, can enhance the effects of modafinil on wakefulness and cognition, and reduce narcoleptic episodes in animal models. These findings suggest that modafinil may exert its therapeutic effects by modulating astroglial connexins.<a class="footnote-ref" id="fnref:44" href="#fn:44">44</a><a class="footnote-ref" id="fnref:45" href="#fn:45">45</a>

<h2 id="further-reading">Further reading</h2>

<ul><li>Stoppini M, Bellotti V, Negri A, Merlini G, Garver F, Ferri G (March 1995). "Characterization of the two unique human anti-flavin monoclonal immunoglobulins". European Journal of Biochemistry. 228 (3): 886–93. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1111%2Fj.1432-1033.1995.tb20336.x">10.1111/j.1432-1033.1995.tb20336.x</a> (inactive 22 December 2024). <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7737190">7737190</a>.{{cite journal}}: CS1 maint: DOI inactive as of December 2024 (link)</li>
<li>Eggena M, Targan SR, Iwanczyk L, Vidrich A, Gordon LK, Braun J (May 1996). <a href="https://doi.org/10.4049%2Fjimmunol.156.10.4005">"Phage display cloning and characterization of an immunogenetic marker (perinuclear anti-neutrophil cytoplasmic antibody) in ulcerative colitis"</a>. Journal of Immunology. 156 (10): 4005–11. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.4049%2Fjimmunol.156.10.4005">10.4049/jimmunol.156.10.4005</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8621942">8621942</a>.</li>
<li>Radhakrishna U, Blouin JL, Mehenni H, Mehta TY, Sheth FJ, Sheth JJ, Solanki JV, Antonarakis SE (July 1997). "The gene for autosomal dominant hidrotic ectodermal dysplasia (Clouston syndrome) in a large Indian family maps to the 13q11-q12.1 pericentromeric region". American Journal of Medical Genetics. 71 (1): 80–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2F%28SICI%291096-8628%2819970711%2971%3A1%3C80%3A%3AAID-AJMG15%3E3.0.CO%3B2-R">10.1002/(SICI)1096-8628(19970711)71:1<80::AID-AJMG15>3.0.CO;2-R</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9215774">9215774</a>.</li>
<li>Clausen BE, Bridges SL, Lavelle JC, Fowler PG, Gay S, Koopman WJ, Schroeder HW (April 1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2230361">"Clonally-related immunoglobulin VH domains and nonrandom use of DH gene segments in rheumatoid arthritis synovium"</a>. Molecular Medicine. 4 (4): 240–57. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1007%2Fbf03401921">10.1007/bf03401921</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2230361">2230361</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9606177">9606177</a>.</li>
<li>Kelley PM, Abe S, Askew JW, Smith SD, Usami S, Kimberling WJ (December 1999). "Human connexin 30 (GJB6), a candidate gene for nonsyndromic hearing loss: molecular cloning, tissue-specific expression, and assignment to chromosome 13q12". Genomics. 62 (2): 172–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fgeno.1999.6002">10.1006/geno.1999.6002</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10610709">10610709</a>.</li>
<li>Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (March 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16267">"Shotgun sequencing of the human transcriptome with ORF expressed sequence tags"</a>. Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2000PNAS...97.3491D">2000PNAS...97.3491D</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.97.7.3491">10.1073/pnas.97.7.3491</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16267">16267</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10737800">10737800</a>.</li>
<li>Lamartine J, Munhoz Essenfelder G, Kibar Z, Lanneluc I, Callouet E, Laoudj D, Lemaître G, Hand C, Hayflick SJ, Zonana J, Antonarakis S, Radhakrishna U, Kelsell DP, Christianson AL, Pitaval A, Der Kaloustian V, Fraser C, Blanchet-Bardon C, Rouleau GA, Waksman G (October 2000). "Mutations in GJB6 cause hidrotic ectodermal dysplasia". Nature Genetics. 26 (2): 142–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F79851">10.1038/79851</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11017065">11017065</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:30809494">30809494</a>.</li>
<li>Rash JE, Yasumura T, Dudek FE, Nagy JI (March 2001). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1804287">"Cell-specific expression of connexins and evidence of restricted gap junctional coupling between glial cells and between neurons"</a>. The Journal of Neuroscience. 21 (6): 1983–2000. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1523%2Fjneurosci.21-06-01983.2001">10.1523/jneurosci.21-06-01983.2001</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1804287">1804287</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11245683">11245683</a>.</li>
<li>Lerer I, Sagi M, Ben-Neriah Z, Wang T, Levi H, Abeliovich D (November 2001). <a href="https://doi.org/10.1002%2Fhumu.1222">"A deletion mutation in GJB6 cooperating with a GJB2 mutation in trans in non-syndromic deafness: A novel founder mutation in Ashkenazi Jews"</a>. Human Mutation. 18 (5): 460. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fhumu.1222">10.1002/humu.1222</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11668644">11668644</a>.</li>
<li>del Castillo I, Villamar M, Moreno-Pelayo MA, del Castillo FJ, Alvarez A, Tellería D, Menéndez I, Moreno F (January 2002). <a href="https://doi.org/10.1056%2FNEJMoa012052">"A deletion involving the connexin 30 gene in nonsyndromic hearing impairment"</a>. The New England Journal of Medicine. 346 (4): 243–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1056%2FNEJMoa012052">10.1056/NEJMoa012052</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11807148">11807148</a>.</li>
<li>Smith FJ, Morley SM, McLean WH (March 2002). <a href="https://doi.org/10.1046%2Fj.0022-202x.2001.01689.x">"A novel connexin 30 mutation in Clouston syndrome"</a>. The Journal of Investigative Dermatology. 118 (3): 530–2. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1046%2Fj.0022-202x.2001.01689.x">10.1046/j.0022-202x.2001.01689.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11874494">11874494</a>.</li>
<li>Pallares-Ruiz N, Blanchet P, Mondain M, Claustres M, Roux AF (January 2002). <a href="https://doi.org/10.1038%2Fsj.ejhg.5200762">"A large deletion including most of GJB6 in recessive non syndromic deafness: a digenic effect?"</a>. European Journal of Human Genetics. 10 (1): 72–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.ejhg.5200762">10.1038/sj.ejhg.5200762</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11896458">11896458</a>.</li>
<li>Common JE, Becker D, Di WL, Leigh IM, O'Toole EA, Kelsell DP (November 2002). "Functional studies of human skin disease- and deafness-associated connexin 30 mutations". Biochemical and Biophysical Research Communications. 298 (5): 651–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-291X%2802%2902517-2">10.1016/S0006-291X(02)02517-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12419304">12419304</a>.</li>
<li>Beltramello M, Bicego M, Piazza V, Ciubotaru CD, Mammano F, D'Andrea P (June 2003). "Permeability and gating properties of human connexins 26 and 30 expressed in HeLa cells". Biochemical and Biophysical Research Communications. 305 (4): 1024–33. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-291X%2803%2900868-4">10.1016/S0006-291X(03)00868-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12767933">12767933</a>.</li>
<li>Zhang XJ, Chen JJ, Yang S, Cui Y, Xiong XY, He PP, Dong PL, Xu SJ, Li YB, Zhou Q, Wang Y, Huang W (June 2003). "A mutation in the connexin 30 gene in Chinese Han patients with hidrotic ectodermal dysplasia". Journal of Dermatological Science. 32 (1): 11–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0923-1811%2803%2900033-1">10.1016/S0923-1811(03)00033-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12788524">12788524</a>.</li>
<li>Pandya A, Arnos KS, Xia XJ, Welch KO, Blanton SH, Friedman TB, Garcia Sanchez G, Liu MD XZ, Morell R, Nance WE (2004). "Frequency and distribution of GJB2 (connexin 26) and GJB6 (connexin 30) mutations in a large North American repository of deaf probands". Genetics in Medicine. 5 (4): 295–303. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1097%2F01.GIM.0000078026.01140.68">10.1097/01.GIM.0000078026.01140.68</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12865758">12865758</a>.</li>
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<li>Harris, A, Locke, D (2009). <a href="https://www.springer.com/978-1-934115-46-6">Connexins, A Guide</a>. New York: Springer. p. 574. <a href="/facts/ISBN_(identifier)/15AdSPa9">ISBN</a> 978-1-934115-46-6.</li>
<li>Smith RJ, Sheffield AM, Van Camp G (2012-04-19). "Nonsyndromic Hearing Loss and Deafness, DFNA3 – RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY". <a href="https://www.ncbi.nlm.nih.gov/books/NBK1536/">Nonsyndromic Hearing Loss and Deafness, DFNA3</a>. University of Washington, Seattle. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/20301708">20301708</a>. NBK1536. In GeneReviews</li>
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<li>Der Kaloustian VM (2011-02-03). <a href="https://www.ncbi.nlm.nih.gov/books/NBK1200/">Hidrotic Ectodermal Dysplasia 2</a>. University of Washington, Seattle. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/20301379">20301379</a>. NBK1200. In Adam MP, Everman DB, Mirzaa GM, Pagon RA, Wallace SE, Bean LJH, Gripp KW, Amemiya A (1993). Pagon RA, Bird TD, Dolan CR, et al. (eds.). <a href="https://www.ncbi.nlm.nih.gov/books/n/gene/TOC/">GeneReviews [Internet]</a>. Seattle WA: University of Washington, Seattle. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/20301295">20301295</a>.</li></ul>

<h2 id="external-links">External links</h2>

<ul><li><ul><li><a href="/facts/Online_Mendelian_Inheritance_in_Man/PkW3zCCU">Online Mendelian Inheritance in Man</a> (OMIM): <a href="https://omim.org/entry/604418">Gap Junction Protein, BETA-6; GJB6 - 604418</a></li>
<li><a href="/facts/Online_Mendelian_Inheritance_in_Man/PkW3zCCU">Online Mendelian Inheritance in Man</a> (OMIM): <a href="https://omim.org/entry/148210">Keratitis-Ichthyosis-Deafness Syndrome, Autosomal Dominant - 148210</a></li>
<li><a href="/facts/Online_Mendelian_Inheritance_in_Man/PkW3zCCU">Online Mendelian Inheritance in Man</a> (OMIM): <a href="https://omim.org/entry/601544">Deafness, Autosomal Dominant 3A; DFNA3A - 601544</a></li>
<li><a href="/facts/Online_Mendelian_Inheritance_in_Man/PkW3zCCU">Online Mendelian Inheritance in Man</a> (OMIM): <a href="https://omim.org/entry/129500">Clouston Syndrome - 129500</a></li>
<li><a href="/facts/Online_Mendelian_Inheritance_in_Man/PkW3zCCU">Online Mendelian Inheritance in Man</a> (OMIM): <a href="https://omim.org/entry/220290">Deafness, Autosomal Recessive 1A; DFNB1A - 220290</a></li></ul></li></ul>

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</ol>

GJB6 open-in-new

GJB6