Ask about this productRelated genes to: MYL3 antibody
- Gene:
- MYL3 NIH gene
- Name:
- myosin light chain 3
- Previous symbol:
- -
- Synonyms:
- CMH8, VLC1, MLC1V, MLC1SB
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: MYL3 antibody
Related articles to: MYL3 antibody
- Chickens (Gallus gallus domesticus), one of the most abundant domesticated animals worldwide, are a major source of high-quality protein from their skeletal muscle. The growth and development of skeletal muscle directly determine the meat quality and yield in poultry. Although skeletal muscle exhibit distinct functional specialization across anatomical locations, the transcriptional mechanisms underlying this diversity, especially the postnatal stages of muscle homeostasis maintenance, remain largely unexplored in broilers. Here, to characterize transcriptional regulatory diversity of chicken skeletal muscles, we performed transcriptomic profiling on 55 skeletal muscle samples from 11 anatomical sites of white feather broiler chickens at two specific growth points 61-week-old and 80-week-old of age. Our finding revealed that the expression patterns of HOX gene family were strongly associated with anatomical regions (head, trunk, limbs), confirming region-specific developmental regulation, although the expression profiles of global PCG was mostly indistinguishable among different skeletal muscles. MYH1E and MYH7B were identified as candidate marker for fast-twitch and slow-twitch muscle in chicken, respectively. The MYH1E-correlated genes were enriched in glycolytic pathways, while the MYH7B-correlated genes were involved in oxidative metabolism. Additionally, TPM3, TNNT1, TNNI1, TNNC1, MYL3, and MYL10 may serve as potential indicators of slow-twitch muscle in chicken. Collectively, our findings provided a transcriptional atlas of chicken skeletal muscle that substantially supplementing current knowledge of its molecular diversity across anatomical locations and age stages, offering direct insights into muscle specialization and age-related regulation for poultry breeding and meat production. - Source: PubMed
Publication date: 2026/04/06
Kong FanliWu XinyuZeng BoQi XuLiu ZhengjiangYang RuohanLu LuCao JiaxueFan XiaolanLi HaohuanLi HuaWang ChengdongLi DeshengLi Mingzhou - Hypertrophic cardiomyopathy (HCM) is a common inherited disease and a leading known cause of sudden cardiac arrest in young adults and athletes. While genetic testing has advanced rapidly in the past decade, the yield of genetic testing remains low. The Clinical Genome Resource (ClinGen) initiative has become a leading resource for defining the clinical relevance of genetic variants with expert groups focusing on evaluating the strength of evidence for each HCM implicated gene. With the rise of large biobanks and population databases, genetic discovery has been significantly advanced. However, whether these databases can be used to validate gene-disease associations curated by ClinGen and provide evidence for novel gene-disease associations remains unclear. Here, we utilized a publicly available database containing 748,879 individuals across three large biobanks (All of Us, UK biobank, Mass General Brigham biobank). We tested the association of rare coding variants in each gene in the HCM ClinGen panel with HCM. In total, 38 genes were tested, and Bonferroni correction was applied accordingly. Of the 12 genes with definitive evidence for HCM (e.g., , , , ), 8 (67%) demonstrated nominally significant association with HCM on a population level, and 5 (42%) remained significant after Bonferroni correction, further supporting the validity of these genes in HCM panels. Several definitive genes which are much less commonly affected in HCM (, , , , , , and ) did not pass our Bonferroni corrected-significance threshold, but all had positively associated effect sizes with HCM. No genes deemed to have moderate or limited evidence had any significant associations with HCM even before Bonferroni correction. Altogether, we show that large biobanks and population databases generally recapitulate established gene-disease associations for HCM and support the ClinGen group's gene curations. The utilization of such publicly accessible databases represents an additional tool for assessing gene validity in monogenic cardiac disorders with an established phenotype, although it may have limited sensitivity and should not be solely relied on. - Source: PubMed
Publication date: 2026/03/21
Dababneh Saif FOng KevinYeung DarwinHawkins Nathaniel MKrahn AndrewLaksman ZacharyTadros RafikRoston Thomas M - Protein kinase C alpha (PKCα) is a central signaling molecule implicated in various cellular processes, including viral infections. However, its role in fish viruses, particularly nervous necrosis virus (NNV), remains elusive. Here, we report that PKCα from marine medaka (MmPKCα) facilitates red-spotted grouper NNV (RGNNV) entry by bridging viral receptor marine medaka myosin light chain 3 (MmMYL3, a known RGNNV receptor mediating macropinocytosis) binding to downstream actin dynamics. RGNNV infection upregulates MmPKCα expression and activates its phosphorylation. Gain- and loss-of-function studies demonstrated that MmPKCα enhances NNV entry, dependent on its kinase activity. We found that MmPKCα interacts with the RGNNV capsid protein via its C-terminal (CT) domain. Although MmPKCα localized to the cell surface, it did not function as an RGNNV receptor, evidenced by unaltered viral binding, inability to render non-susceptible cells permissive, and lack of inhibition by anti-PKCα antibodies/recombinant MmPKCα protein. Instead, MmPKCα directly interacts with MmMYL3 and is essential for MmMYL3-mediated macropinocytosis. Furthermore, MmPKCα binds to marine medaka cofilin (MmCFL1/2) through its CT domain and suppresses cofilin phosphorylation at Ser3, thereby activating cofilin and promoting actin rearrangement critical for macropinocytosis. Our study uncovers a novel MmMYL3-MmPKCα-cofilin signaling axis that RGNNV exploits to enter host cells, highlighting PKCα as a potential therapeutic target for controlling NNV infection. - Source: PubMed
Publication date: 2026/02/25
Yao LanYang XiaogangLi HaifengXiong XingchenYi MeishengJia Kuntong - Genetic testing is valuable to confirm molecular diagnosis in nearly 60% of cases suspected of hypertrophic cardiomyopathy (HCM). However, the interpretation of variants, especially those of uncertain significance (VUSs), remains challenging for laboratories and clinicians. In April 2024, the ClinGen Cardiomyopathy Variant Curation Expert Panel (VCEP) adapted the ACMG/AMP criteria for eight of the sarcomeric genes (, , , , , , , and ), providing a refined framework for variant interpretation in these genes. This retrospective study re-evaluated 69 VUSs identified in 84 HCM patients between 2017 and 2024, aiming to resolve uncertainty and reduce the VUS rate. - Source: PubMed
Publication date: 2025/11/29
Caroselli SilviaCorona GiuliaFabiani MarcoManzoni MartinaMicolonghi CaterinaSavio CamillaGermani AldoBragliola StefaniaMaselli ValeriaRubattu SperanzaMusumeci BeatriceTini GiacomoVisco VincenzoPetrucci SimonaNovelli ValeriaPiane Maria - Super-enhancers (SEs) are critical epigenetic regulators of tissue regeneration, yet their interplay with cellular biomechanics during myogenic differentiation remains unexplored. Here, the TPM1 locus, encoding a core actin-stabilizing protein essential for skeletal muscle regeneration, harbors an evolutionarily conserved SE (TPM1_SE) that may bridge epigenetic control and mechanotransduction. In vitro, TPM1_SE deletion impaired myogenic differentiation and diminished expression of both TPM1 and its circular RNA (circRNA) isoform, CircTPM1. Conditional deletion of TPM1_SE significantly reduce muscle mass and delayed regenerative progression. Mechanistically, TPM1_SE drives expression of linear TPM1 mRNA (mice) and CircTPM1 (bovine) via TEAD4-mediated chromatin looping, coordinating cytoskeletal reorganization during myotube formation. These effects are mediated via activation of the canonical PI3K/AKT signaling pathway through interaction with NKX2.2-a pathway mechanosensitive to cellular tension. Loss of TPM1_SE disrupted NKX2.2-PI3K/AKT signaling. Crucially, CircTPM1 directly bound MYH10, enhancing MYL3-dependent actomyosin assembly, which potentiates cytoskeletal reorganization during myotube formation. Collectively, this findings establish TPM1_SE as an evolutionarily conserved hub integrating epigenetic regulation and biomechanical output. While the murine model underscores its therapeutic potential in muscle regenerative medicine, the bovine CircTPM1-mediated mechanism highlights TPM1_SE as a promising target for genetic improvement of meat quality in livestock. - Source: PubMed
Publication date: 2025/11/16
Zhang RuimenFeng WanyouYang YanyanPan YuZou ChaoxiaWang LeyiZhang SanbaoZhao YiminWu YongmeiWang JinlingZou JianweiCen KeheZhang YongwangHuang HanXu YurongZhong LiGong HailongCheng JuanruLiang JingyuanZheng ZihuaJiang QinyangWei JingweiLi HuiLiang MinhuiShi DeshunYang SufangDeng YanfeiWei Yingming