TRIM9 antibody - C-terminal region (ARP34263_P050)
- Known as:
- TRIM9 (anti-) - C-terminal region (ARP34263_P050)
- Catalog number:
- arp34263_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRIM9 antibody - C-terminal region (ARP34263_P050)
Related genes to: TRIM9 antibody - C-terminal region (ARP34263_P050)
- Gene:
- TRIM9 NIH gene
- Name:
- tripartite motif containing 9
- Previous symbol:
- -
- Synonyms:
- SPRING, RNF91
- Chromosome:
- 14q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-08-24
- Date modifiied:
- 2016-10-05
Related products to: TRIM9 antibody - C-terminal region (ARP34263_P050)
Related articles to: TRIM9 antibody - C-terminal region (ARP34263_P050)
- Melanoma is a highly plastic cancer characterized by distinct cellular phenotypes associated with broadly unique gene expression profiles. TRIM9 is a brain-enriched E3 ubiquitin ligase detected in melanoma, but how TRIM9 expression regulates melanoma phenotype is unknown. Using two metastatic human melanoma cell lines and a mouse melanoma model, we found that TRIM9 promoted melanoma proliferation and altered cell morphology. In cell lines, TRIM9 promoted cellular blebbing and negatively regulated adhesion, secretion, and mesenchymal motility. TRIM9 interacted with VASP in melanoma cells, altering VASP modification, localization, and dynamics. In the absence of TRIM9, cells had an altered actin organization and more focal adhesions, where VASP accumulated and exhibited rapid turnover. We find the alterations in actin architecture and adhesion associated with TRIM9 deletion were coincident with increased motile and contractile mesenchymal behavior in vitro. In vivo loss of TRIM9 in melanoma slowed tumor growth and altered metastasis frequency, size, and destination. Our findings indicate TRIM9 alters the proliferative and morphological phenotypes of metastatic melanoma cells to influence disease progression. - Source: PubMed
Publication date: 2026/03/18
Lukasik KimberlyShah Aneri BHo Chris TLi MatthewPatrick G BeckyBrooks JordanRothenfusser SimonBear James EGupton Stephanie L - Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive motor neuron loss. ALS-linked mutations in UBQLN2 promote protein aggregation and disrupt proteostasis, yet the mutation-specific protein interactomes and their functional relevance remain poorly defined. We employed APEX2 proximity labeling, together with affinity enrichment of biotinylated peptides and LC-MS/MS analysis, to profile the interactomes of wild-type UBQLN2 and two ALS-linked variants, UBQLN2 and UBQLN2. We identified 785 unique biotinylated proteins, many of which exhibit augmented enrichment in the proximity proteomes of the two mutants over wild-type UBQLN2. Notably, the E3 ubiquitin ligases TRIM9 and TRIM26 were selectively enriched in the proximity proteome of UBQLN2, which we validated by coimmunoprecipitation followed by Western blot analysis. Fractionation analysis revealed coaccumulation of TRIM9 and TRIM26 with UBQLN2 in the insoluble fraction, consistent with its heightened aggregation propensity. Treatment of UBQLN2-expressing cells with a proteasomal inhibitor led to elevated accumulation of a C-terminal UBQLN2 fragment that is absent in cells expressing wild-type UBQLN2 or its P497S mutant. Individual knockdown of TRIM9 and TRIM26 significantly increased the abundance of the fragment, establishing UBQLN2 as a substrate for TRIM9- and TRIM26-mediated ubiquitinylation and subsequent proteasomal degradation. These findings nominate TRIM9 and TRIM26 as specific interactors of UBQLN2 and as regulators of a previously underexplored C-terminal UBQLN2 fragment, suggesting that impaired clearance of this species may contribute to ALS pathogenesis. - Source: PubMed
Publication date: 2026/01/25
Chen XingyuanCao ZhongwenLiang XiaochenZhao TingWang Yinsheng - [This corrects the article DOI: 10.1155/2023/2942402.]. - Source: PubMed
Publication date: 2025/10/21
- This study investigates the role of ubiquitination-related genes in pancreatic cancer (PC) using single-cell RNA sequencing (scRNA-seq), spatial transcriptomics, and multi-omics approaches. scRNA-seq data (GSE155698) from PC samples identified 12 cell types, with endothelial cells exhibiting high ubiquitination scores (High_ubiquitin-Endo) and enriched interactions with fibroblasts/macrophages via WNT, NOTCH, and integrin pathways. Spatial transcriptomics (GSE235315) validated cell-type localization. Mendelian randomization (SMR) analysis prioritized TRIM9 as a PC-protective gene, downregulated in tumors and correlated with better survival. WGCNA revealed TRIM9-co-expressed modules linked to prognosis. A machine learning-based prognostic model (CoxBoost+RSF) integrating seven genes (TSPAN6, TSC1, RNF167, PBXIP1, LRRC49, KATNAL2, IGF2BP2) stratified patients into high/low-risk groups with distinct survival, mutation burdens, and immune infiltration. TRIM9 overexpression suppressed PC cell proliferation/migration , while knockdown enhanced malignancy. Mechanistically, TRIM9 promoted K11-linked ubiquitination and proteasomal degradation of HNRNPU, dependent on its RING domain. , TRIM9 overexpression reduced tumor growth, rescued by HNRNPU co-expression. Integrated analyses highlight TRIM9 as a tumor suppressor and prognostic biomarker, mediated via ubiquitination-dependent regulation of HNRNPU stability. This work provides insights into ubiquitination-driven PC pathogenesis and therapeutic targeting. - Source: PubMed
Publication date: 2025/09/19
Chen LiangYing XiaomeiMa ChenfengTang QikaiChen Shuai - Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of RING-type E3 ubiquitin ligases and are attractive targets for the development of novel degraders that exploit the ubiquitin-proteasome pathway. More than half of all TRIM family members contain a PRYSPRY domain, a potentially druggable protein interaction module, located in their C-terminal region. Here, we have determined crystal structures of the PRYSPRY domains from nine TRIM family proteins: TRIM1 (MID2), TRIM9, TRIM10, TRIM11, TRIM15, TRIM16, TRIM18 (MID1), TRIM36, and TRIM67. These structures reveal conservation of the overall β-sandwich topology, despite low sequence conservation, with a unique subdomain swap observed in TRIM11. Significant variations were found in the loops flanking the canonical substrate-binding site, which modulate the shape and electrostatic properties of the binding pocket, hinting at substantial differences in substrate specificity and binding modes among family members. TRIM36 features a unique structural motif between the canonical β-strands 2 and 3, leading to the formation of a dimer, with the canonical substrate-binding site partially occluded by the dimerization motif. In addition, we mapped the locations of missense mutations in MID1 associated with X-linked Opitz syndrome, suggesting that some of these mutations impair the conformational stability of the protein. Taken together, our data provide intriguing insights into the structural and functional divergence of TRIM family PRYSPRY domains, their potential druggability and substrate recognition, and the challenges of ligand design. - Source: PubMed
Publication date: 2025/07/30
Zhubi RezartChaikuad ApiratMuñoz Sosa Christian JJoerger Andreas CKnapp Stefan