Ask about this productRelated genes to: CCDC50 antibody
- Gene:
- CCDC50 NIH gene
- Name:
- coiled-coil domain containing 50
- Previous symbol:
- C3orf6, DFNA44
- Synonyms:
- Ymer
- Chromosome:
- 3q28
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-31
- Date modifiied:
- 2019-04-23
Related products to: CCDC50 antibody
Related articles to: CCDC50 antibody
- Dengchuan cattle, the only dairy-purpose breed among Chinese indigenous yellow cattle, possesses strong environmental adaptability, tolerance to coarse forage, and excellent disease resistance. Its milk contains high levels of protein, fat, and total solids. However, intensive crossbreeding with high-yield Holstein cattle has drastically shrunk its population and increased inbreeding, pushing this valuable breed to the brink of extinction. - Source: PubMed
Publication date: 2026/05/20
Feng KunjiangLiu YongyanLi YamanYang MeiHuang ZongyouWen LingyueXiao HengChen Shanyuan - Cerebrospinal fluid amyloid beta 42, total tau, and phosphorylated tau 181 are well accepted markers of Alzheimer's disease. These biomarkers better reflect disease pathogenesis compared to clinical diagnosis. Here, we perform a genome wide association study meta-analysis including 18,948 individuals of European ancestry and identify 12 genome-wide significant loci across all three biomarkers, eight of them novel. We replicate the association of biomarkers with APOE, CR1, GMNC/CCDC50 and C16orf95/MAP1LC3B. Novel loci include BIN1 for amyloid beta and GNA12, MS4A6A, SLCO1A2 with both total tau and phosphorylated tau 181, as well as additional loci on chr. 8, near ANGPT1 and chr. 9 near SMARCA2. We also demonstrate that these variants have significant association with Alzheimer's disease risk, disease progression and/or brain amyloidosis. The associated genes are implicated in lipid metabolism independent of APOE, coupled with autophagy and brain volume regulation driven by total tau and phosphorylated tau 181 dysregulation. - Source: PubMed
Publication date: 2026/04/21
Timsina JigyashaJiang ChenyangMcCartney Daniel LTao FeifeiDalmasso Maria CarolinaNajar JennaAnastasi FedericaOhlei OlenaPuerta Fuentes RaquelYang ChenyuBradley JosephWestern DanielAli MuhammadWang CiyangYang ChengranWu YingLiu MenghanBudde JohnWilliams JulieMahoney RebeccaCastillo Morales AtahualpaHohman Timothy JDumitrescu LoganWang Ting-ChenTesi Niccolo'Kern SilkeWaern MargdaSkoog Ingmarvan Harten ArgondePijnenburg Yolande A Lvan der Flier Wiesje MSánchez-Juan PascualRodriguez-Rodriguez EloyKleineidam LucaPeters OliverSchneider AnjaKüçükali FahriBellenguez CélineGrenier-Boley BenjaminHeikkinen Samide Rojas ItziarRujescu DanScherbaum NorbertHausner LucreziaDüzel EmrahGrimmer TimoWiltfang JensVandenberghe RikEngelborghs SebastiaanHeilmann-Heimbach StefanieSchmid MatthiasTegos ThomasScarmeas NikolaosDols-Icardo OriolMoreno FerminPérez-Tur JordiBullido María JSánchez-Valle RaquelÁlvarez VictoriaGarcía-González PabloMir PabloReal Luis MPiñol-Ripoll GerardGarcía-Alberca Jose MaríaSeelaar HarroRamakers InezPapma JanneHulsman MarcLaske ChristophTeipel StefanPriller JosefPerneczky RobertBuerger KatharinaNöthen Markus MLewczuk PiotrKornhuber JohannesHampel HaraldGiegling InaGoldhardt OliverDiehl-Schmid JanineAndrade VictorHeneka Michael MtFrölich LutzVogelgsang JonathanGraff CarolineThonberg HakanUllgren AbbePapenberg GoranDeleuze Jean-FrançoisDufouil CaroleWagner MichaelJessen FrankHolstege Hennevan Duijn CorneliaLebouvier ThibaudHannon OlivierLeinonen VilleSoininen HilkkaHerukka Sanna-KaisaGiedraitis VilmantasLöwenmark MalinKilander LenaGenius PatriciaRodríguez BlancaLuckett Emma SNavarro ArcadiCano AmandaMarquié MartaBlennow KajZetterberg HenrikLleo AlbertoBoada MercèRuiz AgustinLee Virginia Man-YeeVan Deerlin Vivianna MDeming YuetivaJohnson Sterling CEngelman Corinne DPastor PauAlvarez IgnacioPeskind Elaine RHeslegrave Amanda JSaykin Andrew JNho KwangsikSchindler Suzanne EMorris John CHoltzman David MMcDade EricRenton Alan EGoate AlisonIbanez LauraRiemenschneider MatthiasAlbert Marilyn SLaws Simon MPorter TenielleO'Brien Eleanor KShaw Leslie MTijms Betty MIngelsson MartinVisser Pieter JelleHiltunen MikkoSleegers KristelRitchie Craig WSims RebeccaBelloy MichaelLambert Jean-CharlesVilor-Tejedor NataliaFernández Maria VictoriaLi Qingqin SNagle Michael WMarioni Riccardo ERamirez AlfredoBertram Larsvan der Lee Sven JCruchaga Carlos - Selective macroautophagy/autophagy is a critical component of innate antiviral defense, relying on selective autophagy receptors to recognize viral cargo and deliver it for lysosomal degradation. In our recent study, we demonstrated that porcine deltacoronavirus (PDCoV) evades this pathway through its NSP5 protease. We uncovered a previously unrecognized antiviral function of the selective autophagy receptor CCDC50, which recognizes K63-linked polyubiquitinated PDCoV envelope (E) protein at lysine 72 and mediates its autophagic degradation, thereby restricting viral replication. This antiviral mechanism operates independently of the canonical receptors SQSTM1/p62 and NBR1. We further demonstrate that PDCoV NSP5 cleaves CCDC50 at glutamine 171, a conserved cleavage site also targeted by NSP5 orthologs from porcine epidemic diarrhea virus/PEDV, transmissible gastroenteritis virus/TGEV, and SARS-CoV-2. This cleavage disrupts the interaction of CCDC50 with ubiquitin and MAP1LC3/LC3, thereby impairing autophagic degradation of the E protein. Collectively, these findings establish CCDC50 as a selective autophagy receptor with antiviral activity against coronaviruses and reveal that coronavirus NSP5 promotes infection by proteolytically dismantling receptor-mediated antiviral autophagy.: CCDC50: coiled-coil domain containing 50; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; NBR1: NBR1 autophagy cargo receptor; NSP5: nonstructural protein 5; PDCoV: porcine deltacoronavirus; SQSTM1/p62: sequestosome 1. - Source: PubMed
Publication date: 2026/04/20
Li KeWei HongyunYin WenqiuZhou PengJin HuiJongkaewwattana AnanSuolang SizhuZhou HongboLuo Rui - Selective autophagy is a critical host defense mechanism that eliminates viral components through lysosomal degradation during coronavirus infection. Coronaviruses (CoVs), however, deploy countermeasures that disrupt this process, and several underlying mechanisms remain unresolved. Here, we identify the autophagy receptor CCDC50 as a substrate of the coronavirus-encoded NSP5 protease. During porcine deltacoronavirus (PDCoV) infection, NSP5 cleaves CCDC50 at glutamine 171 (Q171), a conserved site also processed by NSP5 from PEDV, TGEV, and SARS-CoV-2. Functionally, CCDC50 restricts PDCoV replication by recognizing the envelope (E) protein when it is modified with K63-linked polyubiquitin at lysine 72 (K72) and routing it for autophagic degradation, independently of canonical receptors such as SQSTM1/p62 and NBR1. NSP5-mediated cleavage disrupts CCDC50 interaction with LC3 and ubiquitin, reduces its capacity to target E for degradation, and thereby compromises its antiviral activity. Taken together, our study identifies CCDC50 as a previously uncharacterized antiviral autophagy receptor in coronavirus infection and reveals that PDCoV circumvents this defense through NSP5-mediated cleavage to promote productive infection.IMPORTANCEIn our study, we investigated the interplay between host autophagy pathways and coronavirus infection. We identified the selective autophagy receptor CCDC50 as a potent antiviral factor that suppresses porcine deltacoronavirus (PDCoV) replication. We demonstrated that CCDC50 specifically recognizes the viral envelope (E) protein and targets it for autophagic degradation, thereby restricting the virus. However, we also uncovered a sophisticated viral escape mechanism. We found that PDCoV's main protease, NSP5, cleaves CCDC50 directly at a specific residue, glutamine 171. This proteolytic event impairs the ability of CCDC50 to interact with ubiquitin and the core autophagy machinery, effectively neutralizing its antiviral function and promoting viral replication. Significantly, we determined this to be a highly conserved strategy among coronaviruses. Our findings show that the NSP5 proteases of other divergent coronaviruses, including PEDV, TGEV, and even SARS-CoV-2, all target the same conserved site in CCDC50. These results reveal a common mechanism that coronaviruses use to subvert selective host autophagy. - Source: PubMed
Publication date: 2026/03/12
Li KeWei HongyunZhao KangliChen DongSun YuZhou PengJin HuiJongkaewwattana AnanSuolang SizhuWang DangZhou HongboLuo Rui - During the development of sepsis, aberrant dendritic cell (DC) pyroptosis results in a significant decrease in the numbers of DCs and immune dysfunction. However, the molecular mechanisms regulating DC pyroptosis in sepsis remain unclear. Emerging evidence indicates that RETREG1/FAM134B (reticulophagy regulator 1) is involved in the regulation of programmed cell death to maintain cell viability. Therefore, this study aimed to investigate the potential role and regulatory pathways of RETREG1 in DC death during sepsis. We found that the upregulation of RETREG1 upon septic challenge was intimately associated with the maintenance of immune function. Depletion of RETREG1 in DC significantly aggravated DC pyroptosis and sepsis-induced immune dysfunction by activating the CASP3 (caspase 3)-GSDME (gasdermin E) signaling pathway. Mechanistically, defective RETREG1 expression inhibited autophagic degradation of the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), resulting in abnormal activation of STING1 (stimulator of interferon response cGAMP interactor 1), which further induced CASP3-GSDME-dependent pyroptosis. Genetic downregulation of prevented the activation of STING1 and GSDME-mediated pyroptosis by disturbing ERGIC structure. These results suggest a novel RETREG1-based protective mechanism against DC-mediated immune impairment during sepsis. Genetic or pharmacological modulation of RETREG1 May represent a promising therapeutic strategy for treating sepsis-induced immune suppression.Abbreviations: 7-AAD: 7-aminoactinomycin D; ANXA5/annexin V: annexin A5; ARF1: ARF GTPase 1; ATP: adenosine triphosphate; CALCOCO1: calcium binding and coiled-coil domain 1; CASP1: caspase 1; cC3: cleaved CASP3; CCDC50: coiled-coil domain containing 50; CD274/PD-L1: CD274 molecule; CFSE: carboxyfluorescein diacetate succinimidyl ester; CGAS: cyclic GMP-AMP synthase; CLP: cecal ligation and puncture; DC: dendritic cell; DEGs: differentially expressed genes; DEPs: differently expressed proteins; ER: endoplasmic reticulum; ERGIC: endoplasmic reticulum-Golgi intermediate compartment; GO: Gene Ontology; GOLGA2/GM130: golgin A2; GSDMD: gasdermin D; GSDME: gasdermin E; GSEA: Gene set enrichment analysis; IFN-I: type I interferon; IKK: IκB kinase; IL2: interleukin 2; IRF3: interferon regulatory factor 3; ITGAX/Cd11c: integrin subunit alpha X; KEGG: Kyoto Encyclopedia of Genes and Genomes; LMAN1/ERGIC53: lectin, mannose binding 1; LPS: lipopolysaccharide; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MAP3K7/TAK1: mitogen-activated protein kinase kinase kinase 7; NFKB/NFκB: nuclear factor kappa B; NLRP3: NLR family pyrin domain containing 3; PBMCs: peripheral blood mononuclear cells; PBS: phosphate-buffered saline; PCD: programmed cell death; PINK1: PTEN induced kinase 1; PRKN: parkin RBR E3 ubiquitin protein ligase; PRRs: pattern recognition receptors; PYCARD/ASC: PYD and CARD domain containing; RETREG1/FAM134B: reticulophagy regulator 1; SAMHD1: SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1; SEC62: SEC62 preprotein translocation factor; SQSTM1/p62: sequestosome 1; STEEP1: STING1 ER exit protein 1; STING1: stimulator of interferon response cGAMP interactor 1; TBK1: TANK binding kinase 1; TGFB/TGFβ: transforming growth factor beta; TMED9: transmembrane p24 trafficking protein 9; TLR4: toll like receptor 4; TNF: tumor necrosis factor; T: regulatory T cells; VAP: VAMP associated protein. - Source: PubMed
Publication date: 2026/03/20
Duan YuHe Peng-YiZhu Cheng-LongLi Jin-RuChen YuZheng Li-YuFan QiLing HuaWang LuWu Meng-YaoHan Ze-XinLi TaoYao Yong-MingDai Xin-GuiYao Ren-Qi