Ask about this productRelated genes to: TEX264 antibody
- Gene:
- TEX264 NIH gene
- Name:
- testis expressed 264
- Previous symbol:
- -
- Synonyms:
- ZSIG11, FLJ13935
- Chromosome:
- 3p21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-12
- Date modifiied:
- 2016-10-05
Related products to: TEX264 antibody
Related articles to: TEX264 antibody
- Skeletal muscle atrophy is a pathological condition characterized by the progressive loss of muscle mass and function, driven by factors such as disuse, inflammation, and aging. While the ubiquitin-proteasome system is established as the central mediator of myofibrillar protein degradation, the role of selective autophagy and the degradation of organelles remains underexplored in this context. To address this, we employed a quantitative, time-resolved analysis of protein synthesis and degradation in C2C12 myotubes undergoing TNF-α-induced atrophy, using dynamic Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) coupled with LC-MS/MS. Our data challenges the classical view of atrophy as a uniform, degradation-centric process. Instead, we reveal temporally distinct patterns of selective protein turnover, including differential degradation of myofibrillar, ribosomal, and endoplasmic reticulum (ER)-resident proteins. Early atrophy is characterized by suppressed short-term protein synthesis, increased ubiquitin-ligase expression, proteasomal activation, and ribosome turnover. In contrast, late atrophy features proteasome-dependent myofibrillar protein degradation, selective synthesis, and degradation of mitochondrial and cytoplasmic ribosomes, indicative of metabolic adaptation. Moreover, we identify a temporal shift in autophagic selectivity: from ER homeostasis to a stress-induced ER-degradation program. Notably, autophagy inhibition during atrophy leads to the accumulation of ER-phagy receptors Tex264 and Calcoco1, implicating ER-phagy as a key contributor to atrophic remodeling and highlighting receptor-mediated selective autophagy as a regulatory axis in muscle proteostasis. By elucidating the role of ER-phagy, this study opens avenues for therapeutic interventions targeting proteostasis in inflammation-induced muscle-wasting, contributing to a refined understanding of muscle atrophy beyond proteasomal degradation, particularly in acute inflammatory conditions such as sepsis. - Source: PubMed
Publication date: 2026/04/14
Dueren Ursula KWei Alan An JungGressler A ElisabethRapp SimonPopp OliverKerridge RobertBuonomo VivianaGrumati PaoloMertins PhilippSelbach MatthiasSimon Anna KatharinaSommer Thomas - Stimulator of interferon response cGAMP interactor (STING), the central transducer of the cGAS-STING signaling axis, governs type I interferon (IFN-I) production that is essential for antiviral innate immunity. Modulating STING activity and stability offers potential therapeutic strategies for viral and autoimmune diseases. Here, we demonstrate that testis-expressed protein 264 (TEX264), an endoplasmic reticulum-selective autophagy (ER-phagy) receptor, shows upregulated expression following Herpes simplex virus 1 (HSV-1) infection. Overexpression of TEX264 inhibits the activation of IFN-I signaling triggered by HSV-1 or poly(dA:dT), and enhances HSV-1 replication. Mechanistically, TEX264 interacts with WIPI2 to induce ER-phagy, leading to the degradation of STING and the negative regulation of the IFN-I response. Our findings position TEX264 as a critical regulator of the innate immune response to DNA viruses. - Source: PubMed
Publication date: 2026/03/30
Chang HuasongCha HailiYang RukunQi WenjingWang HongmeiHe Hongbin - High expression of Lysine-Specific Demethylase 5B (KDM5B) in lung cancer drives tumorigenesis and immunosuppression. KDM5B is negatively correlated with endoplasmic reticulum (ER)-phagy receptors such as TEX264, indicating that selective induction of ER-phagy may degrade KDM5B. Our work revealed that chemotherapeutic drug Teniposide (Ten) was a potent anti-lung cancer agent, which could increase the stability of TEX264. The present study aims to elucidate the critical target and mechanism by which Ten inhibits KDM5B through TEX264-associated ER-phagy against lung cancer. Ten exhibited potent lung cancer suppression ability, as evidenced by the weakened proliferation of organoids and tumor grafts in mice along with activation of the immune microenvironment. Highly-expressed KDM5B demonstrated down-regulation upon Ten treatment, which may be attributed to its degradation via ER-phagy. Blockage of ER-phagy weakened Ten-mediated KDM5B degradation. Insightful investigations discovered that Ten activated OTUD3, a deubiquitylase, which stabilized TEX264, a crucial receptor for ER-phagy. Notably, genetic knockdown of TOP2A impacted little on the Ten-mediated ER-phagy. OTUD3 silencing dampened Ten-driven ER-phagy and KDM5B inhibition. To summarize, these findings demonstrate that Ten effectively inhibits lung cancer and activates immunocytes by KDM5B inhibition, which is regulated by TEX264-associated ER-phagy. Most importantly, OTUD3 serves as an essential target for enhancement of TEX264 stabilization. - Source: PubMed
Publication date: 2026/02/26
Han NingYu Xin-RanLi Liu-GenHu JunLeng FanWang LeiYu Ting-TingXu Hua-ZhenHuang HongyaoLi Tong-FeiChen Xiao - The endoplasmic reticulum (ER) is a central organelle for protein synthesis and folding, lipid metabolism and calcium signaling, etc. To maintain ER homeostasis, cells employ a specific autophagy process termed ER-phagy (reticulophagy), which depredates ER components via three forms: macro-ER-phagy (involving bulk ER sequestration), micro-ER-phagy (lysosome-direct), and ER-to-lysosome-associated degradation (ERLAD). The identification of specific ER-phagy receptors including FAM134A, FAM134B, FAM134C, TEX264, SEC62, RTN3L, CCPG1, ATL3, CALCOCO1 and others has significantly advanced our understanding of ER quality control mechanisms. In this review we summarize the current knowledge on ER-phagy receptors, and emerging evidence linking ER-phagy dysfunction to various disease pathologies including neurological disorders, cancer, metabolic diseases, cardiovascular diseases, infections and immune disorders. Recent evidence shows that ER-phagy receptors can form novel ER-derived structures, such as ER-tubular bodies (ER-TBs) consisted of ATL3 and RTN3L, which mediate Golgi-bypassing unconventional protein secretion under stress conditions, revealing non-degradative functions of these receptors beyond quality control. Targeting ER-phagy receptors may provide insights into potential therapeutic strategies for diseases associated with this fundamental cellular process. - Source: PubMed
Publication date: 2026/01/27
Yang Wen-JingSheng Rui - This study aimed to investigate the effect of corilagin(Cor) on the formation of foam cells derived from J774A.1 macrophages and to explore its underlying mechanism based on the endoplasmic reticulum stress(ERS)-endoplasmic reticulum autophagy(ER-phagy) pathway. J774A.1 macrophages were used as the research model and divided into the control group, oxidized low-density lipoprotein(ox-LDL) group, tunicamycin(TM) group, and Cor treatment groups with different concentrations. Cell proliferation activity was assessed using the MTT assay. Intracellular lipid droplet accumulation was observed by oil red O staining. The levels of total cholesterol(TC) and free cholesterol(FC) in cells, as well as interleukin-6(IL-6) and monocyte chemoattractant protein-1(MCP-1) in the cell supernatants, were measured using enzyme-linked immunosorbent assay(ELISA). Intracellular reactive oxygen species(ROS) levels and apoptosis were analyzed by flow cytometry. The interaction between Cor and the eukaryotic translation initiation factor 2α(eIF2α) target protein was predicted by molecular docking. The expression levels of ERS-and autophagy-related proteins were detected by Western blot. The results showed that, compared with the model group, Cor dose-dependently reduced intracellular lipid droplets. The cholesterol ester(CE)/TC ratio was significantly decreased in the low-, medium-, and high-dose Cor groups, indicating reduced lipid deposition. In the high-dose Cor group, the levels of inflammatory cytokines IL-6 and MCP-1 in the supernatant were significantly reduced. In addition, intracellular ROS levels and apoptosis rates were markedly decreased. The optimal binding affinity between Cor and eIF2α was-8.4 kcal·mol~(-1). Furthermore, the high-dose Cor significantly downregulated the expression levels of phosphorylated(p)-eIF2α/eIF2α, activating transcription factor 4(ATF4), glucose-regulated protein 78(GRP78), C/EBP homologous protein(CHOP), nuclear factor-κB(NF-κB), Bcl-2-associated X protein(Bax), and testis expressed gene 264(Tex264), while upregulating the expression level of B-cell lymphoma-2(Bcl-2). In conclusion, Cor inhibits the formation of macrophage-derived foam cells by regulating the expression of proteins in the eIF2α-ATF4-Tex264 signaling pathway, thereby suppressing ERS-induced excessive ER-phagy and apoptosis in macrophages. - Source: PubMed
Wu Jing-YiHong Yu-BingHu Meng-MengMa Chao-JieLi ChenZhao YiChe Yan-Yun