Ask about this productRelated genes to: MDFIC antibody
- Gene:
- MDFIC NIH gene
- Name:
- MyoD family inhibitor domain containing
- Previous symbol:
- -
- Synonyms:
- HIC, MDFIC1
- Chromosome:
- 7q31.1-q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-22
- Date modifiied:
- 2018-02-13
Related products to: MDFIC antibody
Related articles to: MDFIC antibody
- PIEZO channels are critical for sensory mechanotransduction. While MyoD-family inhibitor proteins were identified as PIEZO1 auxiliary subunits, their broader regulatory roles, particularly in sensory cells, remained unclear. Here, we demonstrate native MDFIC and MDFI regulate endogenous PIEZO channel currents in various nonsensory cell types. However, neither MDFIC nor MDFI are expressed in primary sensory neurons. In these cell types, we identified an uncharacterized third member of this family, /, that shares the ability to physically bind to PIEZO1 and PIEZO2. MDFIC2 is selectively expressed in subsets of mechanosensitive neurons, including dorsal root ganglia, trigeminal ganglia, and vagal sensory neurons. Like its paralogues, MDFIC2 alters PIEZO1/2 mechanosensitivity and inactivation kinetics, converting them into high-threshold slowly inactivating mechanoreceptors. Extensive cryo-EM reveals a conserved binding pocket for these auxiliary subunits in the pore modules of both PIEZO1 and PIEZO2 mediated by the posttranslationally modified distal C termini of MyoD-family inhibitor proteins. This structural and functional characterization of MyoD-family inhibitor proteins as PIEZO1/2 channel auxiliary subunits offers insights into the mechanobiology of nonsensory and sensory cells. - Source: PubMed
Publication date: 2026/04/09
Zhou ZijingDai FeiCheng DelfineMa XiaonuoOmidkhoda Seyedeh FarzanehClarke JackZhang HuijingLaden MichaelGuo YangLi Jinyuan VeroLiu RenjingWong Emily SZhang YixiaoCox Charles D - Attention-deficit/hyperactivity disorder (ADHD) is a common heritable neurodevelopmental disorder, affecting ~7 million children (11.4%) in the U.S. However, ADHD's underlying genetic architecture remains largely unknown. Transcriptome-wide association studies (TWAS), which integrate expression quantitative trait loci (eQTL) and GWAS summary data, can identify differentially expressed risk genes underlying complex phenotypes. Here we conduct a TWAS of ADHD using expression data from multiple brain tissues to improve understanding of the complex genetic architecture underlying this psychopathology. - Source: PubMed
Publication date: 2026/02/22
Abrishamcar SarinaDai QileYang JingjingHüls AnkeEpstein Michael P - The gene encodes connexin 37 or Gap junction protein alpha-4. Gap junction proteins are required for lymphatic valvulogenesis. It is known that homozygous knockout of the Gja4 gene in mice leads to lymphatic system dysfunction and absent venous valves. In this report, we identify for the first time a homozygous nonsense variant in the gene, c.97delC (transcript ID NM_002060.3) or p.Arg33Alafs*98, or chr1:g.34794309delC (GRCh38 format) in a human fetus with increased nuchal fold thickness and abnormal fetal ductus venosus termination. Asymptomatic parents were carriers of the same variant. Additionally, a search of the literature showed that this specific variant in the gene has not been previously documented as a cause of human fetal disease. A STRING (Search Tool for Retrieval of Interacting Genes/Proteins) database analysis showed close interactions between the gene and other genes involved in the causation of hereditary lymphedema: and . However, STRING database analysis also showed no interaction of the gene with genes in the rasopathy pathway, which can also be causative of increased fetal nuchal translucency, namely and . Thus, we describe a novel gene-human fetal phenotype association. - Source: PubMed
Publication date: 2025/11/17
Chauhan BinodiniPrajapati Nilamben ASagarkar SnehaMenon PramilaKachhadiya TusharVaniawala ShalinVaniawala SalilTamhankar VasundharaTamhankar Parag M - PIEZO channels are mechanical force sensors involved in various biological processes, including somatosensation. To date, only a few PIEZO-binding partners have been identified, including MyoD-family inhibitor proteins (MDFI and MDFIC). Here, we show that MDFIC2, a third member of the MDFI protein family with an as-yet-unknown function, is expressed in a subset of nociceptive sensory neurons. MDFIC2 modulates both PIEZO1 and PIEZO2 gating properties by slowing their kinetics and shifting mechanical sensitivity to higher forces. Interestingly, is downregulated in mouse neuropathic pain models in which mechanical allodynia is a hallmark symptom. We found that intrathecal administration of adeno-associated virus vector encoding cDNA reduces mechanical sensitivity and attenuates mechanical allodynia in the spared nerve injury neuropathic pain model. These findings demonstrate a mechanism for regulating mechanosensation and highlight a potential therapeutic route for treating mechanical allodynia. - Source: PubMed
Publication date: 2025/11/07
Habib Abdella MLi ShengnanZhang ChenjingJi MeijunOsorio NancyPenalba VirginieTorres Jesus MGossage Samuel JRezai Mehdi AGeard Amy FRahim Ahad AMahmoud Ahmed M MSantana-Varela SoniaZhou JunZhao JingWood John NOkorokov Andrei LZhou XuelongCox James JCoste Bertrand - PIEZO channels transmit mechanical force signals to cells, allowing them to make critical decisions during development and in pathophysiological conditions. Their fast/slow inactivation modes have been implicated in mechanopathologies but remain poorly understood. Here, we report several near-atomic resolution cryo-EM structures of fast-inactivating wild-type human PIEZO1 (hPIEZO1) and its slow-inactivating channelopathy mutants with or without its auxiliary subunit MDFIC. Our results suggest that hPIEZO1 has a more flattened and extended architecture than curved mouse PIEZO1 (mPIEZO1). The multi-lipidated MDFIC subunits insert laterally into the hPIEZO1 pore module like mPIEZO1, resulting in a more curved and extended state. Interestingly, the high-resolution structures suggest that the pore lipids, which directly seal the central hydrophobic pore, may be involved in the rapid inactivation of hPIEZO1. While the severe hereditary erythrocytosis mutant R2456H significantly slows down the inactivation of hPIEZO1, the hPIEZO1-R2456H-MDFIC complex shows a more curved and contracted structure with an inner helix twist due to the broken link between the pore lipid and R2456H. These results suggest that the pore lipids may be involved in the mechanopathological rapid inactivation mechanism of PIEZO channels. - Source: PubMed
Publication date: 2025/07/16
Shan YuanyueGuo XinyiZhang MengmengChen MeiyuLi YingZhang MingfengPei Duanqing