TRIM16 antibody - N-terminal region (ARP35802_P050)
- Known as:
- TRIM16 (anti-) - N-terminal region (ARP35802_P050)
- Catalog number:
- arp35802_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRIM16 antibody - N-terminal region (ARP35802_P050)
Related genes to: TRIM16 antibody - N-terminal region (ARP35802_P050)
- Gene:
- TRIM16 NIH gene
- Name:
- tripartite motif containing 16
- Previous symbol:
- -
- Synonyms:
- EBBP
- Chromosome:
- 17p12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-22
- Date modifiied:
- 2016-10-05
Related products to: TRIM16 antibody - N-terminal region (ARP35802_P050)
Related articles to: TRIM16 antibody - N-terminal region (ARP35802_P050)
- Influenza A virus (IAV) exhibits notable genetic diversity and cross-species transmission capacity, posing a continuous challenge to public health. Elucidating host immune regulatory mechanisms is crucial for identifying new antiviral targets that can overcome viral resistance. Here, using human A549 lung epithelial cells as the primary model, we identify fibroblast growth factor 8 (FGF8) as a crucial host factor whose expression is significantly elevated during infection by various IAV subtypes (including H1N1, H13N2, H9N2, and PR8). Through gain- and loss-of-function assays, we demonstrate that FGF8 specifically enhances viral replication at the post-entry stage by suppressing interferon-beta (IFN-β) and interferon-stimulated genes (ISGs) expression. Mechanistically, FGF8 reduces retinoic acid-inducible gene I (RIG-I) protein stability via K48-linked polyubiquitination without affecting its mRNA levels. Ubiquitination identifies Lysine 258 (K258) on RIG-I as the essential modification site; notably, a K258R mutation prevents RIG-I degradation and restores IFN-β induction. Furthermore, TurboID-based proximity labeling captures the close spatial association of FGF8 with both tripartite motif containing 16 (TRIM16) and RIG-I, revealing that FGF8 acts as a molecular scaffold to recruit the E3 ligase TRIM16 to RIG-I. Consistently, TRIM16 silencing replicates the antiviral effects of FGF8 knockdown. Collectively, our findings demonstrate that FGF8 recruits TRIM16 to degrade RIG-I, thereby facilitating viral immune evasion. Disrupting this interaction offers a potential avenue for anti-influenza A virus intervention. - Source: PubMed
Publication date: 2026/05/22
Wei RanZhang HuixiaCheng KaihuiWang SongYuan ZhenMa SisiYu Zhijun - SARS-CoV-2 accessory protein ORF3a contributes to viral pathogenesis through membrane remodeling, immune evasion, and inflammation induction. However, the molecular mechanisms underlying ORF3a-mediated pathogenesis remain poorly characterized, and no therapeutic strategies targeting ORF3a currently exist. Here, we demonstrate that palmitoylation, a post-translational modification, governs ORF3a-mediated viral pathogenesis. Specifically, ORF3a undergoes ZDHHC18-mediated palmitoylation at evolutionarily conserved Cys130/Cys133 residues, which stabilizes the protein by masking an intrinsic proteasomal degradation signal. This palmitoylation competitively inhibits tripartite motif-containing 16 (TRIM16)-dependent K27-linked polyubiquitination, thereby preventing ORF3a degradation and enhancing viral replication and inflammatory responses. A designed ORF3a-mimicking palmitoylation-inhibitory peptide (OPIP) blocked ORF3a palmitoylation, promoted its degradation, and significantly reduced SARS-CoV-2 pathogenicity. Collectively, these findings establish ZDHHC18-mediated palmitoylation as a central regulator of ORF3a stability and virulence, revealing a potentially druggable axis for disrupting SARS-CoV-2 pathogenesis. - Source: PubMed
Publication date: 2026/05/10
Yang SidiLi KunLiu LihongZeng LinsenDeng QifengHuang JiachengDong XiaoranWang XinLiang JianweiLiu HongchaoPeng HongLin YuxinXie XiaoluYe YuzhenXu TiefengWang ZhaohuanLi Chun-MeiGuo Deyin - TAR DNA-binding protein 43 (TDP43) aggregation is a well-established pathological hallmark of amyotrophic lateral sclerosis (ALS) and related neurodegenerative disorders, contributing significantly to oxidative stress and neuronal injury. Here, we report that the M337V mutation in TDP43 exacerbates its proteotoxicity relative to the wild-type protein. Concurrently, multi-omics analysis revealed a pronounced downregulation of TRIM16 in motor neuron-like cells expressing either wild-type or M337V mutant TDP43. Functional studies demonstrated that TRIM16 overexpression effectively mitigated oxidative stress, restored mitochondrial integrity, and suppressed ferroptosis. Mechanistically, TRIM16 promoted the ubiquitination and degradation of Keap1, thereby facilitating the activation of Nrf2-mediated antioxidant genes. Furthermore, we identified the iron import receptor TFR1 as a novel ubiquitination substrate of TRIM16. TRIM16 mediated the ubiquitination of TFR1 and targeted it for p62-dependent autophagic degradation, which in turn reduced iron accumulation and lipid peroxidation. Collectively, our findings establish TRIM16 as a pivotal suppressor of TDP43-induced toxicity by orchestrating dual cytoprotective pathways to enhance cellular resilience, highlighting its promising therapeutic potential for TDP43 proteinopathy. - Source: PubMed
Publication date: 2026/05/05
Chen QiuyuZhou YujunPeng YuchenLan JiaqiKang YuyingWu LeiLiu JiaoTang JingshuPeng Ying - Aging increases susceptibility to various diseases, including cardiac injury. Which leads to cardiac dysfunction by increasing myocardial fibrosis and mitochondrial dynamics disorder. However, the molecular mechanisms in the aging heart have not been elucidated. The E3 ligase TRIM16 (tripartite motif-containing protein 16) functions as a regulator to alleviate cardiac injury. Sirt6 has been shown to play a cardioprotective role by maintaining mitochondrial dynamics. Our study aimed to elucidate the molecular mechanisms of the TRIM16-Sirt6-Mfn2 signaling pathway in the aging heart. We used aged mice and performed intracardiac injections of AAV-TRIM16/Sirt6. The results demonstrated that TRIM16 improved cardiac function by increasing Sirt6 expression in the aging heart. Further in vitro studies were conducted using D-galactose-cultured h9c2 cells to explore the relationship between TRIM16/Sirt6 and mitochondrial dynamics. The findings showed that TRIM16/Sirt6 protected D-galactose-cultured h9c2 cells by promoting Mfn2-dependent mitochondrial fusion and enhancing mitochondrial respiratory capacity. In conclusion, our results confirm that TRIM16 activation improves cardiac function via the Sirt6/Mfn2 signaling pathway in the aging heart. This study provides evidence that TRIM16/Sirt6/Mfn2 signaling plays a novel protective role in the aging heart and offers a promising therapeutic strategy for age-related heart failure. - Source: PubMed
Publication date: 2026/05/03
Chen YawuGuo HongDing XiaochenLu LinheJin Ping - Age-related macular degeneration (AMD) is a global vision threatening disease affecting the macular region of the retina. AMD is classified into two forms: dry and wet AMD. There are no effective treatment options available for dry AMD (80% of cases). The cellular pathology includes oxidative stress and dysfunctional autophagy challenging the homeostasis of the retinal pigment epithelial (RPE) cells. Clinical findings include the formation of drusen deposits beneath the RPE cells consisting of 42 amino acids long amyloid beta (Aβ) among other components. However, the origin of drusen remains elusive. The 5xFAD (familiar Alzheimer's disease) mouse model of Alzheimer's disease produces abundant levels of Aβ making it an interesting model to study the possible relationship of Aβ to the formation of extracellular deposits and AMD-like pathology. An immunohistology analysis of the 5xFAD mouse model showed accumulation of autophagic markers SQSTM1 (sequestosome 1) and ubiquitin in the RPE. Concurrently, the markers of secretory autophagy enabling the delivery of the intracellular material to the extracellular lumen were upregulated. Aβ, SQSTM1, ubiquitin, catalase, and TRIM16 (tripartite motif containing 16) shifted age-dependently from intracellular origin to drusen-like deposits beneath the RPE cells. Additionally, classical proteins secreted via secretory autophagy, IL-1β (interleukin 1β), HMGB1 (high mobility group box-1), and ferritin showed similar accumulation which became visible in fundus age-dependently. These findings suggest a role for Aβ in the cellular pathogenesis of AMD. Furthermore, this model showed activated secretory autophagy pathway suggesting a role for Aβ in drusen-like deposition formation. - Source: PubMed
Ruuth JohannaTamminen ToniToropainen ElisaTanila HeikkiHyttinen Juha M TMalm TarjaKaarniranta KaiKoskela Ali