B5 Receptor _ PCID1 _ EIF3M Antibody
- Known as:
- B5 Receptor _ PCID1 _ EIF3M Antibody
- Catalog number:
- AF1132a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- B5 Receptor _ PCID1 EIF3M Antibody
Related genes to: B5 Receptor _ PCID1 _ EIF3M Antibody
- Gene:
- EIF3M NIH gene
- Name:
- eukaryotic translation initiation factor 3 subunit M
- Previous symbol:
- PCID1
- Synonyms:
- hfl-B5, FLJ29030, GA17, eIF3m, TANGO7
- Chromosome:
- 11p13
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-31
- Date modifiied:
- 2015-12-04
Related products to: B5 Receptor _ PCID1 _ EIF3M Antibody
Related articles to: B5 Receptor _ PCID1 _ EIF3M Antibody
- Phosphodiesterase 3A (PDE3A) modulators such as anagrelide induce complex formation between PDE3A and Schlafen 12 (SLFN12), selectively killing cancer cells that co-express both proteins. As PDE3A forms isoform- and cell type-specific signalosome complexes across multiple subcellular compartments, the effects of its modulation are expected to depend strongly on the surrounding protein interaction network. However, despite considerable pre-clinical and early clinical interest in PDE3A modulators, the cellular context in which these compounds act has remained poorly characterized. Using proximity-dependent biotinylation in two human cancer cell lines (SA-4, liposarcoma; HeLa, cervical adenocarcinoma), we mapped the interactomes of PDE3A, SLFN12, and the anagrelide-induced PDE3A-SLFN12 complex. Anagrelide induced 259 high-confidence interactions, most notably with ribosomal proteins and translation initiation factors, while suppressing 877 interactions, most prominently those associated with the proteasome, protein folding, and the ER membrane. Interactions were selectively induced with peripheral eukaryotic translation initiation factor 3 (eIF3) subunits eIF3A and eIF3B, while interactions with core eIF3 subunits eIF3H, eIF3L, and eIF3M were suppressed. These findings were validated by native co-immunoprecipitation across three cancer cell lines, and multiplex immunofluorescence confirmed accumulation and ribosomal redistribution of both PDE3A and SLFN12 following anagrelide treatment. AlphaFold modeling of the PDE3A-SLFN12 complex with a partial 43S pre-initiation complex predicted binding near eIF3B and the eIF2αβγ-tRNA ternary complex at the mRNA entry channel. By mapping the interactomes surrounding the drug-induced complex, our study provides important mechanistic context for how PDE3A modulators act within the cell. In our proposed model, anagrelide remodels the interactome of the PDE3A-SLFN12 complex, which relocalizes and accumulates near the mRNA entry channel of the 43S pre-initiation complex. - Source: PubMed
Publication date: 2026/09/18
Salmikangas SamiLindholm IinaSultana NasrinMerikoski NannaToivanen KirsiLiu XiaonanVarjosalo MarkkuBöhling TomVesterinen TiinaSihto Harri - The reprogramming of myocardial energy metabolism is critical for cardiac repair after ischemia/reperfusion (I/R) injury, yet the upstream translational control mechanisms remain elusive. Here, through multi-omics analysis of human failing hearts, we identify the mRNA regulator eIF3m as an essential factor for maintaining cardiac glycolytic flux post-I/R. We show that eIF3m, independently of the canonical eIF3 complex, stabilizes Mt2 and related stress-response mRNAs, ultimately protecting the key glycolytic activator Pfkfb3. Loss of eIF3m impairs the heart's adaptive shift toward utilizing glycolysis for energy, leading to contractile dysfunction. Mechanistically, eIF3m deficiency exacerbates excessive nitro-oxidative stress, which damages and inactivates the key glycolytic enzyme Pfkfb3. This damage is counteracted by the metallothionein Mt2, a direct binding partner of eIF3m. Our findings reveal the eIF3m-Mt2 axis as a novel translational checkpoint that governs metabolic reprogramming and nitrative stress resistance in the injured heart, nominating it as a potential therapeutic target for myocardial I/R injury. - Source: PubMed
Publication date: 2026/08/08
Wei ZilunZhao YongchaoJia DaileGao RifengXiong WeidongSun XiaoleiWeng XinyuLiu BowenSong ShuaiLuo WeiCui JianHu KaiSun AijunGe Junbo - End-stage chronic liver disease in children is associated with sarcopenia and aberrant adipose tissue mass. We investigated correlations between liver pathology-associated gene pathways (fibrosis, inflammation and steatosis) and metabolic genes in muscle and adipose tissue. - Source: PubMed
Publication date: 2026/07/06
Kyrana EiriniZhang ChengJin HanSalehi SiamakWells Jonathan C KDeheragoda MaeshaMitry Ragai RDhawan Anil - Triple-negative breast cancer (TNBC) represents a particularly aggressive form of breast tumors. Mitochondrial dysfunction represses the proliferation of TNBC cells. Ubiquitin-specific proteases 34 (USP34) has been predicted to be abnormally overexpressed in TNBC. This research examined the role of USP34 in the mitochondrial function modulation of TNBC. Herein, cell proliferation was evaluated by the 5-ethynyl-2'-deoxyuridine assay. Mitochondrial membrane potential was detected employing the JC-1 assay. Mitochondrial superoxide was measured utilizing MitoSOX Red assay. Mito‑Tracker Red CMXRos staining was selected to monitor mitochondrial network structure. The relationship among USP34, eukaryotic translation initiation factor 3 m (eIF3m), and mitochondrial carrier homolog 2 (MTCH2) was validated by co-immunoprecipitation, GST-pull down, RNA immunoprecipitation and RNA-pull down analysis. We found that USP34 silencing inhibited cell proliferation by inducing mitochondrial dysfunction in TNBC cells. USP34 maintained the stability of the eIF3m protein through deubiquitination. Overexpression of eIF3m countered the mitochondrial dysfunction induced by USP34 silencing. Furthermore, eIF3m upregulated the MTCH2 level by directly binding to its 5'UTR region. MTCH2 overexpression reversed the damaging effect of eIF3m silencing on mitochondrial function. Collectively, USP34 maintained the stability of eIF3m protein through deubiquitination; the upregulated eIF3m bound to the 5'UTR of MTCH2 mRNA to promote MTCH2 expression, thereby maintaining mitochondrial function and promoting the malignant progression of TNBC. - Source: PubMed
Publication date: 2026/04/23
Qian Peng-FeiZeng YiZhong Wang-Jing - Eukaryotic initiation factors (eIFs), a bunch of proteins that deeply involved in translation initiation of mRNA in eukaryotes, are closely associated with physiological and pathological processes. eIF3m, a core subunit in eIF3 complex, also played critical roles in virus infection. In this study, a co-immunoprecipitation coupled with mass spectrometry (Co-IP/MS) was performed to identify host factors that interacted with ORF1B, a unique non-structural protein of fowl adenovirus serotype 4 (FAdV-4). Among 2502 cellular proteins, eIF3m, especially its C-terminal part, was verified to interact with ORF1B and these two proteins co-localized in the cytoplasm. Importantly, overexpression of eIF3m promoted FAdV-4 replication in LMH cells, whereas knockdown eIF3m exerted an opposite effect. Collectively, these findings indicate that ORF1B hijacked eIF3m to positively participate in FAdV-4 infection. - Source: PubMed
Publication date: 2026/01/31
Wang ZengLi RuixueZhai SaiminGao HuichaoLiu KeyingYang XiaZhao JunZhang Xiaozhan