Ask about this productRelated genes to: UNC13A antibody
- Gene:
- UNC13A NIH gene
- Name:
- unc-13 homolog A
- Previous symbol:
- -
- Synonyms:
- KIAA1032, Munc13-1
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-16
- Date modifiied:
- 2016-10-05
Related products to: UNC13A antibody
Related articles to: UNC13A antibody
- We devised a quantitative scoring function to assess the cumulative effects of somatic nonsynonymous single-nucleotide variants (SNVs) on protein-coding genes in patients with ovarian cancer (OvCa) and thyroid cancer (ThCa). The goal is to find novel candidate cancer-related genes for downstream bioinformatics analyses and wet-lab studies. With the Genomic Data Commons as primary data resource, SNV information was extracted from whole-exome sequencing data from patients with these cancers. A cumulative variant scoring function, (), was developed to sum up the deleterious effects of the individual SNVs on gene . While () can be computed using any popular functional effect analyzers such as FATHMM-XF, SIFT, PolyPhen, and CADD, we have also established an integrative scoring function () that combines the deleterious assessments from different analyzers and demonstrated that () is a more effective method for identifying likely cancer-related genes. Based on the () rankings, the top three novel genes for OvCa are , , and and those for ThCa are , , and . Furthermore, the top 1% genes with highest () scores for each cancer were submitted for KEGG pathway analysis. The results revealed that several genes of the family within the type II diabetes mellitus pathway are likely related to both OvCa and ThCa and suggested other molecular interactions that should be further studied in connection with OvCa prognosis and ThCa treatment. - Source: PubMed
Publication date: 2026/03/26
Bataycan AmandaNurudeen OmodolapoMohl Jonathon EMitchell Khodeza BegumLeung Ming-Ying - Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder marked by progressive motor neuron loss, leading to muscle weakness, paralysis, and respiratory failure. Dysregulation of RNA metabolism and splicing has emerged as a central mechanism in ALS pathogenesis. TARDBP (TAR DNA-binding protein), FET family proteins (FUS, EWSR1, TAF15), SOD1 (Superoxide Dismutase 1), and C9orf72 (Chromosome 9 Open Reading Frame 72) are key genes associated with ALS that regulate RNA processing, alternative splicing, and nuclear-cytoplasmic transport. Mutations or mislocalization of these proteins result in nuclear loss-of-function and cytoplasmic gain-of-function toxicity, promoting protein aggregation, sequestering spliceosomal components, and impairing spliceosome assembly. This leads to the aberrant inclusion of cryptic exons in essential neuronal genes, such as STMN2 (Stathmin 2) and UNC13A (Unc-13 Homolog A), resulting in the production of truncated proteins, defective axonal maintenance, and impaired synaptic function. TDP-43 pathology, a hallmark of ALS, disrupts splicing and RNA transport, while C9orf72 repeat expansions and FET protein mutations exacerbate cytoplasmic aggregation and stress granule dynamics. Mutant SOD1 contributes via mitochondrial dysfunction, endoplasmic reticulum stress, and disrupted axonal transport. Therapeutic strategies targeting these mechanisms are advancing rapidly. Gene replacement therapy, which restores STMN2 expression, and antisense oligonucleotides (ASOs) targeting mutant transcripts show promise in preclinical and early clinical studies. Complementary approaches, including the inhibition of stress kinases and the activation of autophagy, reduce cytoplasmic protein aggregation and support neuronal homeostasis. This review provides a comprehensive overview of RNA splicing regulation, spliceosomal dysfunction, and cryptic exon incorporation in ALS. Understanding the interplay among splicing defects, RNA-binding protein pathology, and neuronal degeneration is critical for developing next-generation multimodal therapies to restore RNA processing, reduce toxic protein accumulation, and promote motor neuron survival. - Source: PubMed
Publication date: 2026/04/09
Priya RatnaTanti Goutam KumarJain Buddhi Prakash - Immunohistochemically (IHC) measured transactive response DNA-binding protein 43 (TDP-43) inclusions are observed in Alzheimer's disease (AD) and are associated with medial temporal lobe atrophy. Accumulation of cryptic exons occurs in AD in response to TDP-43 pathology. We aimed to assess relationships between IHC and biochemically measured insoluble TDP-43 and cryptic exons and assess associations with hippocampal and amygdala volume loss and atrophy rates on magnetic resonance imaging (MRI). - Source: PubMed
Publication date: 2026/04/08
Youssef HossamGatto Rodolfo GGhayal Nikhil BEstades Ayuso VirginiaJansen-West Karen RDunmore Judith ASong YupingYue MeiCook Casey NDeTure MichaelRawlinson Bailey DCastanedes-Casey MonicaJack Clifford RPetersen Ronald CDickson Dennis WPetrucelli LeonardWhitwell Jennifer LPrudencio MercedesJosephs Keith A - Synaptic vesicle (SV) release probability () is determined by two probabilistic factors: the probability of release sites being occupied by fusion-competent, well-primed SVs and their fusion probability (). While recent studies emphasize SV priming as a key mechanism underlying functional synaptic diversity, disentangling priming from fusion is notoriously challenging. Here we developed a mouse genetic approach for inducible and selective increase of SV priming. A histidine-to-lysine mutation at position 567 of Munc13-1 increases its function. Combining this mutation with a Cre-dependent removal of the wild-type Munc13-1 allele enables cell type-selective enhancement of Munc13-1 function. This manipulation increased excitatory postsynaptic current amplitude at hippocampal synapses exclusively through elevating without affecting release site number or quantal size. A sequential, two-step priming model predicts that the enhanced results from an elevated proportion of well-primed SVs, without altering . Last, we provide unequivocal evidence that the postsynaptic target cell type-dependent variability in presynaptic glutamate release is mainly the consequence of variability in SV priming. - Source: PubMed
Publication date: 2026/04/08
Aldahabi MohammadBalint FloraLorincz AndreaLipstein NoaBrose NilsNusser Zoltan - Neurotransmitter release requires the precise localization and assembly of the SNARE machinery at presynaptic release sites. Although liquid-liquid phase separation of active zone scaffolds is known to organize these sites, the mechanism for the specific enrichment of the SNARE machinery has remained unclear. In this study, we establish that within RIM1/RIM-BP2 biomolecular condensates, Munc13-1 functions as an organizational hub that spatially sorts and concentrates cognate SNAREs, orchestrating their stepwise assembly. In particular, this condensate environment empowers Munc13-1 to cluster Syb2 into nanodomains on the vesicle membrane, dramatically increasing local SNARE density and ensuring efficient complex formation. Consequently, the introduction of RIM1/RIM-BP2 into PC12 cells enhances spatiotemporally precise dense-core vesicle exocytosis in a Munc13-dependent manner. Our findings suggest a model in which phase separation creates a privileged platform that enables Munc13-1 to direct SNARE complex assembly, thereby ensuring the speed and precision of synaptic vesicle exocytosis. - Source: PubMed
Publication date: 2026/04/07
Zhang HongZhang YuZhao ZhifeiCao ZelinZhao KexuLei MengshiWang ShenMa Cong