CLCC1 antibody
- Known as:
- CLCC1 (anti-)
- Catalog number:
- orb125583
- Product Quantity:
- 200 ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- CLCC1 antibody
Related genes to: CLCC1 antibody
- Gene:
- CLCC1 NIH gene
- Name:
- chloride channel CLIC like 1
- Previous symbol:
- -
- Synonyms:
- MCLC
- Chromosome:
- 1p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-08-04
- Date modifiied:
- 2017-08-18
Related products to: CLCC1 antibody
Related articles to: CLCC1 antibody
- Beta-coronavirus infection disrupts endoplasmic reticulum (ER) homeostasis; however, the mechanisms by which viral proteins manipulate ER-resident factors remain unclear. Here, we report that the SARS-CoV-2 accessory protein ORF3a binds to the ER chloride channel CLCC1, thereby impairing ER ion homeostasis, activating the unfolded protein response, and inducing endomembrane remodeling. Using newly developed ratiometric reporters, we showed that this interaction exacerbated the basal levels of ER-phagy and nucleophagy. Importantly, CLCC1 counteracted ORF3a by sequestering it within the ER, attenuating its toxicity and suppressing viral replication, which established CLCC1 as a host restriction factor. We further elucidated a spatiotemporal mechanism: during early infection, ORF3a accumulates in the ER, co-assembles with CLCC1 into puncta, and disrupts ER homeostasis; at the later stage, ORF3a overload enables its escape from CLCC1-mediated ER retention and subsequent translocation to lysosomes, facilitating viral egress. This ER-centric function is conserved across diverse beta-coronaviruses, including SARS-CoV-1 and bat- or pangolin-derived strains, revealing a unified pathogenic strategy. Furthermore, in mouse brains, the ORF3a-CLCC1 axis recapitulates key neuropathological features, including ER stress, autophagic dysfunction, neuronal death, and neuroinflammation, providing a mechanistic link to COVID-19-associated neurological symptoms. Our findings identify CLCC1 as an essential host defense protein and establish a conceptual framework to guide future research on antiviral responses at the organelle level and related disease mechanisms. - Source: PubMed
Publication date: 2026/09/15
Guo LiangHuang BaoyingYu HanzhiXu YiWei LeiZheng JijieLi YuanzheWu DiZhao PengWu ChangchengTan WenjieJia Yichang - DYT1 dystonia is an incurable movement disorder caused by a loss-of-function mutation in Torsin1A, an endoplasmic reticulum (ER)-resident AAA+ ATPase. Here, we use Drosophila and human cells to shed light on Torsins' mode of action. Fly germ cells lacking dTorsin arrest in development with defects in nuclear pore complex (NPC) biogenesis due to impaired nuclear envelope membrane fusion. We identify the conserved membrane protein Chloride Channel CLIC-like protein 1 (CLCC1) as a Torsin1A interaction partner whose absence phenocopies membrane fusion defects caused by Torsin deletion. CLCC1 is enriched at membrane fusion sites, and molecular dynamics (MD) simulations suggest that CLCC1 rings induce bilayer remodeling and lipid flux to initiate fusion of the outer and inner nuclear membranes. Remarkably, CLCC1 overexpression rescues defects associated with loss of Torsins, indicating that a main role of dTorsin/Torsin1A is to sustain CLCC1 functionality. Our findings inform a model of nuclear envelope membrane fusion and imply that modulating CLCC1 expression is a promising therapeutic prospect for DYT1 dystonia. - Source: PubMed
Publication date: 2026/08/04
Maslennikova DariaBaird HarryDing XinyueKumar AshutoshLoffreda AlessiaRamachandran KausthubhKösters Benjamin JonasBos Jelmi Uit deAshiono CarolineFrischer-Ordu KatharinaLuithle NaemiUliana FedericoDey GautamKorkhov Volodymyr MAntonin WolframVanni StefanoJagannathan MadhavKutay Ulrike - The TMEM41B scramblase and its regulatory partner CLCC1 initiate lipid flux by equilibrating newly synthesized phospholipids across the endoplasmic reticulum (ER) bilayer, a fundamental process required for diverse events ranging from membrane biogenesis to bulk lipid supply. Loss of CLCC1/TMEM41B causes ER bilayer imbalance, which induces giant ER-enclosed lipid droplets (geLDs) and drives rapid progression into severe metabolic-dysfunction-associated steatohepatitis (MASH). Combining both human cell lines and mouse models, we herein reveal CLCC1 to be the long-missing client of the luminal torsin ATPases, which selectively engage oligomerized CLCC1 at sites of ER bilayer imbalance. Mice hepatic torsinA inactivation triggers geLD formation amid disrupted lipoprotein biogenesis and severe MASH, closely phenocopying CLCC1/TMEM41B deficiency. Mechanistically, torsins act as assembly-promoting ATPases that drive CLCC1 oligomerization for its recruitment to imbalanced bilayers. Remarkably, ectopic CLCC1 expression reverses cellular and systemic lipid disorders arising from hepatic torsinA deficiency. Hence, torsin ATPases emerge as fundamental regulators that organize CLCC1 and the downstream TMEM41B scramblase to govern lipid partitioning and membrane homeostasis. - Source: PubMed
Publication date: 2026/08/04
Wang YonglunWang RenqianYao YuanhangHou RongxianYan LuLin YiechangHu YatingLi YouleiWu LingzhiZhu YuangangGao NingSong ChenWang XiaoJi ZhejianChen Xiao-Wei - The nuclear pore complex (NPC) serves as the central transport gateway between nucleus and cytoplasm. NPC biogenesis requires the assembly of over 500 proteins culminating in the fusion of the inner and outer nuclear membranes. The mechanism of membrane fusion is unknown. Here, we elucidate how Brl1 and Brr6 mediate membrane fusion in S. cerevisiae. Our data suggest that both proteins form ring-shaped complexes with membrane-remodeling activity. Brl1 localizes to NPC assembly sites via a nuclear export sequence and interacts with Brr6 across the nuclear envelope through conserved hydrophobic loops. Disrupting this interaction blocks fusion and halts NPC assembly. Molecular dynamics simulations suggest that the Brl1-Brr6 complex drives membrane fusion by forming a channel across the bilayers enabling lipid exchange. Phylogenetic analyses and functional experiments in human cells and D. melanogaster establish CLCC1 as the NPC fusogen in metazoans. Together, our results uncover a conserved membrane fusion mechanism in eukaryotes. - Source: PubMed
Publication date: 2026/07/09
Fischer Jonas SWojtynek MatthiasKumar AshutoshBaird HarryRadilová KateřinaMaslennikova DariaRamachandran KaustubhBecker Anna NAgote-Aran ArantxaLoffreda AlessiaKralt AnnemarieJagannathan MadhavDey GautamKutay UlrikeVanni StefanoWeis Karsten - PIGBOS is a recently identified 54-amino acid microprotein localized to the mitochondrial outer membrane and implicated in the endoplasmic reticulum (ER) stress response. Here, we identify a previously unrecognized role for PIGBOS in cellular Ca homeostasis. Manipulation of PIGBOS expression in HEK293T cells revealed that PIGBOS enhances Ca signaling by promoting ER Ca release through inositol 1,4,5-trisphosphate (IP) receptors and subsequent mitochondrial Ca uptake in response to histamine stimulation. In contrast, siRNA-mediated depletion or genetic ablation of PIGBOS markedly attenuated these responses. PIGBOS influenced Ca transfer from the ER to mitochondria without affecting direct mitochondrial Ca uptake and also promoted store-operated Ca entry. Functional analyses demonstrated that the interaction of PIGBOS with the ER-resident chloride channel CLCC1 via its C-terminal region is required for this activity. Network analysis predicted a direct association between PIGBOS and CLCC1, as well as indirect connections with core Ca signaling components, including IP receptors, STIM1, Orai1, and SERCA, whose expression was altered upon modulation of PIGBOS abundance. Loss of PIGBOS impaired mitochondrial respiration, reduced ATP production, and increased reactive oxygen species. Together, these findings establish PIGBOS as a key regulator of ER-mitochondrial Ca signaling that couples Ca dynamics to mitochondrial bioenergetics and cellular stress responses. - Source: PubMed
Publication date: 2026/06/25
Aditya SeemantiBera Amal Kanti