Ask about this productRelated genes to: IFITM3 antibody
- Gene:
- IFITM3 NIH gene
- Name:
- interferon induced transmembrane protein 3
- Previous symbol:
- -
- Synonyms:
- 1-8U, DSPA2b
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 2000-02-11
- Date modifiied:
- 2018-03-08
Related products to: IFITM3 antibody
Related articles to: IFITM3 antibody
- The interferon-induced transmembrane proteins (IFITMs) are a family of potent broad-spectrum antiviral factors that restrict enveloped viruses primarily by altering the biophysical properties of membranes, thereby preventing viral-cellular fusion. While their antiviral mechanisms are well established, increasing evidence suggests that IFITMs can also play important roles in cancer biology by remodeling of the cancer cell surface proteome and by modulating signaling pathways involved in proliferation, cell survival, and metastasis. In this review, we summarize the diverse biological functions attributed to IFITMs over the years; we highlight the salient aspects of their biology; and we propose a unifying conceptual framework in which seemingly diverse functions of IFITMs in virology and cancer biology can be understood through their capacity to regulate the behavior of membranes. - Source: PubMed
Publication date: 2026/06/17
Xia TingtingCimarelli Andrea - Growing epidemiological and mechanistic evidence indicates that infections substantially increase the risk of Alzheimer's disease (AD) and related dementias. Systemic immune activation and pathogen persistence may act as upstream triggers accelerating neurodegenerative cascades. - Source: PubMed
Publication date: 2026/06/15
Barichello TatianaScaini GiselliTayyab MohdDal-Pizzol Henrique RitterPetronilho FabriciaDal-Pizzol Felipe - Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by amyloid-β (Aβ) plaque deposition, neurofibrillary tau tangles, synaptic dysfunction, and progressive cognitive decline. AD is increasingly recognized as a condition in which chronic neuroinflammation actively shifts amyloid precursor protein (APP) processing toward the amyloidogenic pathway, driving Aβ production and accumulation rather than merely accompanying amyloid deposition. In this review, we examine the molecular cross-talk between inflammatory signalling and secretase regulation, highlighting how pro-inflammatory mediators promote amyloidogenic processing and contribute to downstream synaptic dysfunction. We discuss the major pathways linking glial activation to aberrant APP cleavage, including STAT3-dependent BACE1 upregulation, immune-mediated modulation of γ-secretase through IFITM3, and activation of the C/EBPβ/δ-secretase axis, which connects inflammatory stress to both amyloid and tau pathology. We further address the contribution of epigenetic mechanisms, particularly microRNA-mediated derepression of BACE1 and suppression of ADAM10, as well as SIRT3-related impairment of Aβ clearance. These interconnected processes establish a feed-forward pathogenic network in which neuroinflammation amplifies secretase imbalance, amyloidogenesis, and synaptic vulnerability. Finally, we discuss emerging multi-target therapeutic strategies aimed at modulating inflammatory signalling, restoring non-amyloidogenic APP processing, and preserving proteostatic and synaptic resilience. Collectively, this framework supports the view that targeting the inflammatory control of secretase activity may represent a biologically relevant strategy for disease modification in AD. - Source: PubMed
Publication date: 2026/05/27
Cipriano Giovanni LucaAnchesi IvanRaffaele IvanaAstorino Maria FrancescaMinuti AurelioCalabrò MarcoCrisafulli Concetta - Crohn's disease (CD) is a chronic inflammatory bowel disease marked by immune imbalance and monocyte dysfunction. IFITM3, a palmitoylation-related immune protein, may play a role in this process, but its involvement in CD remains unclear. This study aimed to explore the causal role of IFITM3 and related proteins in CD using Mendelian randomization, multi-omics analysis, and machine learning, to identify potential diagnostic markers and therapeutic targets. - Source: PubMed
Publication date: 2026/06/04
Song XinxiaYuan TangyuXing JiayinLiu Pengtao - Interferon-induced transmembrane (IFITM) proteins restrict virus infections at the stage of cellular entry. We previously characterized a GxxxG motif in the CD225 domain of human IFITM3 that mediates its multimerization, which is essential for the reduction of membrane fluidity by IFITM3 and for its antiviral activity against the influenza A virus. Here, using an unbiased approach coupling immunoprecipitation with mass spectrometry, we show that the GxxxG motif is also important for the interaction of IFITM3 with other proteins, including IFITM1. IFITM1 is primarily regarded as a cell surface protein that restricts the entry of viruses fusing at the plasma membrane, but this model is based mostly on overexpression studies and is at odds with some studies showing that it can restrict endocytic viruses. Here, we show that endogenous IFITM1 and IFITM3 co-reside in membranes of acidic late endosomes and lysosomes and interact, as determined by co-immunoprecipitation and proximity ligation assay. Knockdown of endogenous IFITM3 resulted in enhanced localization of IFITM1 to the plasma membrane, indicating that IFITM3 promotes IFITM1 localization to endolysosomes. To assess the antiviral protection conferred by endogenous IFITM1 and IFITM3 against viruses fusing at endolysosomal membranes, we measured cellular infection by influenza A virus. While individual knockdown of IFITM1 or IFITM3 significantly increased infection, combined knockdown of both IFITM1 and IFITM3 boosted infection to a much greater extent. These results suggest that endogenous IFITM1 and IFITM3 restrict Influenza A virus entry in endolysosomes in a cooperative manner. - Source: PubMed
Publication date: 2026/06/09
Wilt IsaiahJolley Abigail ARahman KaziLai Kin KuiAgarwal MaheshShi GuoliAndresson ThorkellCompton Alex A