Ask about this productRelated genes to: FCHO1 antibody
- Gene:
- FCHO1 NIH gene
- Name:
- FCH domain only 1
- Previous symbol:
- -
- Synonyms:
- KIAA0290
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-08
- Date modifiied:
- 2019-02-20
Related products to: FCHO1 antibody
Related articles to: FCHO1 antibody
- Synaptic vesicle (SV) recycling is critical for sustaining neurotransmission. Although FCHO1, a protein containing both an F-BAR domain and a μ-homology (μ-HD) domain, is recognized as a nucleator of clathrin-mediated endocytosis in non-neuronal systems, its physiological role at synapses remains unclear. Here, we investigated the function of FCHO1 in SV endocytosis at central synapses using a combination of shRNA-mediated knockdown and pHluorin-based live imaging. Within defined stimulation paradigms (25-300 action potentials at 10 Hz), depletion of FCHO1 markedly slowed endocytic kinetics across all stimulation intensities and was fully rescued by re-expression of an shRNA-resistant construct. Domain-specific functional analyses revealed stimulation-strength-dependent functional requirements. The F-BAR domain was sufficient to support vesicle retrieval under low stimulation conditions, whereas the μ-homology domain (μ-HD) became essential as stimulation strength increased. These findings support a model in which FCHO1 operates as a demand-sensitive scaffold within the endocytic pathway, with distinct structural domains differentially required as neural activity and consequently endocytic load escalates. Our results establish FCHO1 as a critical regulator of SV endocytosis and suggest that multidomain endocytic proteins may scale their functional contributions according to the magnitude of neuronal activation. - Source: PubMed
Publication date: 2026/04/06
Lee Hyun JungLee WongyoungKim Sung Hyun - - Source: PubMed
Publication date: 2026/02/22
Esenboga SalihaDormus TamerYaz İsmailOkur Fatma VisalCagdas DenizKuşkonmaz Barış - The delivery of nucleic acids into host cells has emerged as an innovative and promising therapeutic approach for various diseases. Despite significant advances in nanoparticle delivery systems, persistent cellular barriers limit the clinical application of most existing technologies. In this study, we developed a programmable device that applies precise uniaxial cyclic stretching to cells cultured on custom polydimethylsiloxane chambers to investigate whether mechanical stimulation can enhance the transfection efficiency (TE) of gold-standard non-viral gene delivery vectors. Applying cyclic mechanical stimulation ( = 0.1 Hz, ε = 10% strain, = 30 min) to HeLa cells and human myoblasts (hMyo) significantly increased nuclear translocation of the mechanosensitive transcription factor Yes-Associated Protein (YAP). Gene expression analysis revealed that this mechanical conditioning orchestrated a coordinated modulation of endocytic machinery, upregulating clathrin-mediated endocytosis (FCHO1) and macropinocytosis (STX1B) pathways while downregulating endocytic inhibitors (DLC1, EHD2). These mechanically induced cellular adaptations resulted in significantly enhanced TE of both plasmid DNA (pDNA)- and mRNA (mRNA)-carrying gold-standard branched polyethylenimine (PEI)-based complexes in both HeLa cells and hMyo, compared to static conditions. Our findings demonstrate that mechanical stimulation is an effective complementary strategy for improving non-viral gene delivery by leveraging endogenous cellular mechanotransduction pathways. Rather than modifying vector chemistry, this mechanobiological approach enhances the performance of existing delivery systems by transiently modulating cellular uptake capacity and nuclear accessibility. This work offers mechanistic insights into how mechanotransduction regulates cellular uptake and highlights opportunities for leveraging controlled mechanical environments in applications such as ex vivo cell engineering. - Source: PubMed
Publication date: 2026/01/08
Fruzzetti FlaminiaRuzzante BeatriceGiagnorio EleonoraBonanno SilviaLauria Pinter GiuseppeMarcuzzo StefaniaCandiani GabrieleBono Nina - Primary immunodeficiency diseases (PIDs) are inherited disorders caused by genetic defects affecting immune function, leading to recurrent infections, autoimmunity, and malignancies. Many PIDs remain genetically uncharacterized, largely due to rare variants with unclear pathogenicity, which complicates the process of establishing an accurate diagnosis. Next-generation sequencing (NGS) technology enables the identification of molecular defects, improving the diagnosis of PIDs. Functional validation of genetic variants identified through PID-related gene screenings is crucial for determining their clinical significance. In this study, we identified five novel variants in PID-related genes in six families using whole-exome sequencing. These variants include FCHO1 (E44K), NCF2 (A206P), NCF2 (c.174 + 1G > A), STAT1 (L199F), and a copy number deletion in LRBA (exon 9-17). Functional validation was performed for four of these variants: STAT1 (L199F) using pSTAT1 assay, NCF2 (A206P and c.174 + 1G > A) by DHR assay, and FCHO1 (E44K) using CRISPR-mediated genome editing. Overall, the present study expands the knowledge of previously unreported variants in primary immunodeficiency. - Source: PubMed
Vr ArvindenGovindaraj Geeta MadathilIyer Aditya RamdasPaul SangitaEdavazhippurath AthulyaJain AbhinavGupta PragyaDeshmukh Gauspasha YusufSingh ShivaniSaravanakumar VinodhBhardwaj JuhiSharma SrishtiBenny Tancia PSaravanan PriyaBhoyar Rahul CImran MohamedSenthivel VigneshwarDivakar Mohit KumarVignesh HarieJolly BaniDalvi AparnaBargir Umair AhmedMadkaikar ManishaBk BinukumarSivasubbu SridharRamalingam SivaprakashScaria Vinod - Super-resolution microscopy achieves a few nanometers resolution, but colocalization analysis in a molecular complex is limited by its labeling density. Here we present a method for quantitative mapping of molecular complexes using multiplexed super-resolution imaging, integrating exchangeable single-molecule localization (IRIS). We developed antiserum-derived Fab IRIS probes for high-density labeling of endogenous proteins and protein cluster coloring (PC-coloring), which employs pixel-based principal component analysis and clustering. PC-coloring maps regions of distinct ratios of multiple proteins, and in each region, correlation between two proteins is calculated for evaluating the complex formation. PC-coloring revealed multi-layered complex formation in a clathrin-coated structure (CCS) prior to endocytosis. Upon epidermal growth factor (EGF) stimulation, EGF receptor (EGFR)-dominant, EGFR-Grb2-complex, and Grb2-dominant regions lined up from outside the CCS rim. Along the interior of Grb2-dominant regions, CCS components (Eps15, FCHo1/2 and intersectin-1) formed a complex with Grb2 away from EGFR. The Grb2-dominant region and Grb2-CCS component complex formation probably determine EGFR recruitment sites in the CCS rim. - Source: PubMed
Publication date: 2025/04/23
Kiuchi TaiKobayashi RyouheiOgawa ShuichiroElverston Louis L HVavylonis DimitriosWatanabe Naoki