FNIP1 Antibody
- Known as:
- FNIP1 Antibody
- Catalog number:
- Y213900
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- FNIP1 Antibody
Related genes to: FNIP1 Antibody
- Gene:
- FNIP1 NIH gene
- Name:
- folliculin interacting protein 1
- Previous symbol:
- -
- Synonyms:
- KIAA1961
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-08-09
- Date modifiied:
- 2016-10-05
Related products to: FNIP1 Antibody
Related articles to: FNIP1 Antibody
- - Source: PubMed
Publication date: 2026/08/05
- Altered energy metabolism is a shared driver across cardiometabolic diseases-the leading cause of death globally. Energy metabolism varies between individuals and is partly heritable. Here, to investigate the genetic basis of energy metabolism, we perform an exome-sequencing analysis of 1,032,116 people from America, Europe and Asia, and estimate associations between rare protein-coding variants and the ratio of triglyceride to high-density-lipoprotein cholesterol (TG:HDL)-an energy-state biomarker that we associate with diverse cardiometabolic risk factors and diseases. We identify 59 independent genes (P < 1.04 × 10) that are enriched for liver- and adipose-expressed master regulators of energy balance, storage and metabolism; 23 (39%) of these genes encode approved or clinical-stage drug targets. Ultra-rare protein-truncating variants in FNIP1 (allele frequency, 0.01%), which encodes a suppressor of energy expenditure and mitochondrial metabolism, are associated with a lower TG:HDL ratio, lower liver fat, lower glycaemia, favourable fat distribution and around 60% lower odds of cardiometabolic disease. FNIP1 knockdown in primary human hepatocytes induces lipid breakdown and lysosomal gene expression, while combined hepatic knockdown of Fnip1 with its paralogue Fnip2 or knockdown of its interactor Flcn protect against weight gain, reduce liver fat and enhance insulin sensitivity in mice fed a high-fat diet. Our study implicates the FNIP1 pathway in human energy metabolism and highlights its inhibition as a potential therapeutic strategy in cardiometabolic disease. - Source: PubMed
Publication date: 2026/08/05
Hindy GeorgeAdam Rene CSosina OlukayodePryce DwaineBlair DavidHerman JosephLee JosephDornbos PeterMayerhofer ErnstGilly ArthurHunt CharleenGeraghty BenjaminLandheer KarlGanel LironBaldassari AntoineZhang ChuanyiMintah IvorySun DaphneCoppola AngelBrown KyleNguyen TramXia Xin Rader Daniel JMelander OlleStill Christopher DBerumen JaimeKuri-Morales PabloAlegre-Díaz JesusTorres Jason MEmberson Jonathan RCollins RoryTapia-Conyer RobertoBalasubramanian SuganthiJones Marcus BLeBlanc Michelle GMurphy Andrew JKyratsous Christos AOverton John DReid Jeffrey GAbecasis Goncalo RMarchini JonathanWiller CristenYancopoulos George DSleeman Mark WBovijn JonasLocke AdamBaras ArisVerweij NiekGusarova ViktoriaLotta Luca A - Metabolic dysfunction-associated steatohepatitis (MASH) is emerging as a leading cause of chronic liver disease. MTOR (mechanistic target of rapamycin kinase) complex 1 (MTORC1) is a potential therapeutic target, whereas suppression of total MTORC1 activity can lead to unwanted effects. Here, we found that byakangelicin (Bya), a natural compound, selectively inhibited MTORC1-mediated phosphorylation of TFEB (transcription factor EB), without affecting canonical MTORC1 substrates. Knockout of hepatic blocked the alleviation effects of Bya on hepatic steatosis, inflammation, insulin resistance, and fibrosis in mice, while reintroduction of TFEB restored these effects. We identified Bya directly bound to MET370 and PHE552 of FLCN (folliculin), suppressing the function of the FLCN-FNIP1 (folliculin interacting protein 1)/FNIP2 complex, which in turn inhibited MTORC1-mediated cytoplasmic sequestration of TFEB. Mutation of FLCN (M370A and F552A) in the liver abolished Bya-induced protection against MASH. Thus, Bya is a promising therapeutic natural compound for MASH, and selective inhibition of MTORC1 is a potential approach to treat this disease. aa, amino acids; AAV, adeno-associated virus; Bio, biotin; Bio-Bya, biotin-conjugated Bya; BSA, bovine serum albumin; BW, body weight; Bya, byakangelicin; CETSA, cellular thermal shift assay; CHIP-atlas, chromatin immunoprecipitation atlas; C, maximum concentration; CQ, chloroquine; DARTS; drug affinity responsive target stability assay; EIF4EBP1/4E-BP1, eukaryotic translation initiation factor 4E binding protein 1; FBS, fetal bovine serum; FDA, food and drug administration; FIMO-JASPAR, find individual motif occurrences-JASPAR; FLCN, folliculin; FNIP1, folliculin interacting protein 1; GAP, GTPase-activating protein; GOT1/AST, glutamic-oxaloacetic transaminase 1; GPT/ALT, glutamic-pyruvic transaminase; GTRD, gene transcription regulatory database; GTT, glucose tolerance test; H&E, hematoxylin and eosin; Hbonds, hydrogen bonds; HFD, high-fat diet; HFHC, high-fat and high-cholesterol; HOMA-IR, homeostatic model assessment of insulin resistance; HSCs, hepatic stellate cells; IP, immunoprecipitation; ITT, insulin tolerance test; K, dissociation constant; KEGG, kyoto encyclopedia of genes and genomes; KPBS, potassium phosphate-buffered saline; LC-MS/MS, liquid chromatography-tandem mass spectrometry; LW/BW, liver-to-body weight ratio; MAP1LC3/LC3, microtubule associated protein 1 light chain 3; MASH, metabolic dysfunction-associated steatohepatitis; MASLD, metabolic dysfunction-associated steatotic liver disease; MCD, methionine and choline deficient; MST, microscale thermophoresis assay; MTOR, mechanistic target of rapamycin kinase; MTORC1, MTOR complex 1; ND, normal diet; NFKB/NF-κB, nuclear factor kappa B; NFKBIA/IKBA, NFKB inhibitor alpha; OP, oleate acid and palmitate acid; PBS, phosphate-buffered saline; PCA, principal component analysis; qRT-PCR, real-time quantitative PCR; RELA/p65, RELA proto-oncogene, NF-kB subunit; Res, resmetirom; Rg, radius of gyration; RMSD, root-mean-square deviation; RMSF, root-mean-square fluctuation; RPS3, ribosomal protein S3; RPS6KB1/S6K1, ribosomal protein S6 kinase B1; RRAGC, ras related GTP binding C; SASA, solvent-accessible surface area; SNRPD2, small nuclear ribonucleoprotein D2 polypeptide; SQSTM1/p62, sequestosome 1; T, half-life; TFE3, transcription factor binding to IGHM enhancer 3; TFEB, transcription factor EB; TMEM192, transmembrane protein 192; VIM, vimentin; WT, wild-type. - Source: PubMed
Publication date: 2026/05/25
Du XiliangFang ZhiyuanLiu GuowenWang LiJu LingxueGao WenwenSong YuxiangLei LinLi Xinwei - Rare coding genetic variants may exert large effects on risk of common disease, yet their contribution to disease architecture and their utility in gene prioritization remain limited by inadequate sample sizes. Here, we performed a massive-scale rare variant association study (RVAS), analyzing over 1.1 million sequenced participants among which 130,000 had atrial fibrillation (AF). Through a multi-mask burden testing approach, we identified 15 genes significantly associated with AF through rare large-effect variation. Integrative analyses revealed strong convergence between genes implicated by rare and common variation, and highlighted instances where RVAS data may aid in GWAS prioritization. Nevertheless, several RVAS genes were not among GWAS loci (, , , ), or were not nominated through contemporary GWAS prioritization (). Finally, we observed that ultra-rare protein-disrupting variants - concentrated in a small number of large-effect size genes - explained at least 2% of AF susceptibility across European and African ancestry groups. These findings refine the genetic architecture of AF, while highlighting the value and cost of RVAS for genomic discovery in common disease. - Source: PubMed
Publication date: 2026/05/04
Jurgens Sean JEnzan NobuyukiDinsmore Ian RChoi Seung HoanLuo JonLipov AlexHartle CassandraWang XinMarston Nicholas AWeng Lu-ChenMelloni Giorgio EmChalazan BrandonGray Michael PPirruccello James PDiaz AnnetteChaffin Mark DOrnelas-Loredo AylinTang OwenDarbar Faisal AKany ShinwanChen Yiningvon Falkenhausen Aenne SMorrison Alanna CNatale AndreaTveit ArnljotGeelhoed BastiaanCade BrianVan Wagoner David RHaase DoreenSoliman Elsayed ZDavogustto Giovanni ECalkins HughAnderson Jeffrey LBrody Jennifer ABarnard JohnHokanson John ESmith Jonathan DBis Joshua CYoung KendraJohnson Linda SbLong LeannRisch LorenzGula Lorne JKwee Lydia CoulterKühne MichaelPreuss MichaelGupta NamrataNafissi Navid ASmith Nicholas LNilsson Peter Mvan der Harst PimWells Quinn SJudy Renae LSchnabel Renate BJohnson ReneeSmit Roelof AjGabriel StaceyKnight StaceyFurukawa TetsushiMin Yuan-IYoneda Zachary TLaksman Zachary WmAlonso AlvaroPsaty Bruce MAlbert Christine MArking Dan ERoden Dan MChasman Daniel IRader Daniel JConen DavidMcManus David DFatkin DianeBoerwinkle EricMarcus Gregory MChristophersen Ingrid ESmith J GustavRoberts Jason DRaffield Laura MShoemaker M BenjaminCho Michael HCutler Michael JChung Mina KOlesen Morten SSinner Moritz FSotoodehnia NonaKirchhof PaulusLoos Ruth JfNazarian SamanMohanty SanghamitraDamrauer Scott MKaab StefanHeckbert Susan RRedline SusanShah Svati HTanaka ToshihiroEbana Yusuke Lubitz Steven ALunetta Kathryn LBenjamin Emelia JRienstra MichielFigtree Gemma ADarbar DawoodBezzina Connie RRuff Christian TSabatine Marc SMirshahi ToorajEllinor Patrick T - Hepatopancreatic microsporidiosis (HPM) in Litopenaeus vannamei caused by Ecytonucleospora hepatopenaei (EHP) mainly manifests as growth retardation. Hitherto, the mechanism by which it inhibits growth remains unclear. In this study, muscle transcriptome sequencing was conducted on shrimp artificially challenged with EHP for 10 d, and the expression characteristics of genes related to the mTOR pathway were investigated to explore the molecular mechanism underlying muscle growth inhibition in EHP-infected shrimp. A total of 1289 differentially expressed genes were identified, including 726 up-regulated and 563 down-regulated genes. Significant down-regulation of growth-related genes was detected in EHP-infected shrimp, especially those encoding actin and myosin. Moreover, the expression levels of cell division-related gene cyclin dependent kinase 1 (CDK1) and the molting-related gene β-N-acetylhexosaminidase 20 (HEX) were also significantly inhibited. However, the gene expression of mTOR and its related negative regulatory factors (unc-51, Tsc1 and FNIP1) was significantly up-regulated, along with immune-related genes such as anti-lipopolysaccharide factor (ALF) and prophenoloxidase-activating factor 3 (PPAF3). In contrast, the expression of NLR family CARD domain containing 4 (NLRC4) was significantly down-regulated. Functional enrichment analyses revealed that EHP infection mainly affected protein synthesis and glucose metabolism pathways. Furthermore, the expression of key genes in the mTOR pathway was detected to be significantly up-regulated within 20 d post EHP challenge. These findings indicate that EHP infection triggered an immune response and disrupted muscle cell division, protein synthesis, and molting processes, providing valuable resources for clarifying the molecular mechanism of growth regulation in shrimp after EHP infection. - Source: PubMed
Publication date: 2026/05/08
He ChuanyuYin ZhipengTian YajieYang FanCao ZhengWang CuixiaYan DongchunLi TingChang LinruiSi Lingjun