Ask about this productRelated genes to: TEX264 Blocking Peptide
- 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 Blocking Peptide
Related articles to: TEX264 Blocking Peptide
- Cadmium (Cd), a well-recognized neurotoxicant, elicits neuronal death and cognitive impairment. Cd cytotoxicity disrupts endoplasmic reticulum (ER) proteostasis, leading to the accumulation of misfolded and unfolded proteins and subsequent ER stress-mediated apoptosis. Endoplasmic reticulum autophagy (ER-phagy) serves as a crucial quality-control mechanism that resolves excessive ER stress and maintains ER homeostasis. However, the precise roles of ER-phagy, ER stress-mediated apoptosis, and their crosstalk in Cd-induced neurotoxicity remain poorly defined. Here, we demonstrated that Cd exposure robustly induces ER stress and the subsequent apoptotic injury in the mouse hippocampus and HT-22 hippocampal neurons. Pharmacological inhibition of ER stress with 4-phenylbutyric acid (4-PBA) effectively rescued Cd-triggered neuronal damage, reduced cell death, and ameliorated Cd-associated cognitive deficits. Notably, Cd exposure leads to pronounced ER-phagy dysfunction, as evidenced by decreased LC3-II accumulation, elevated calnexin levels, and impaired ER-phagy autophagic flux in vivo and in vitro. Furthermore, the ER-phagy receptor TEX264 was downregulated under Cd stress. Importantly, restoration of ER-phagy via overexpressing TEX264 markedly mitigated Cd-elicited ER stress, thereby blocking the downstream apoptotic cascade. Collectively, our findings identify impaired ER-phagy as a previously unrecognized mechanism underlying Cd neurotoxicity, which synergizes with ER stress-mediated apoptosis to promote hippocampal neuronal injury. These results highlight ER quality control pathways as promising therapeutic targets for the intervention of Cd-induced cognitive and neuronal damage. - Source: PubMed
Publication date: 2026/08/29
Gao YufeiCao LuyangHong YiboKe HaoYuan QuanHu JunXu QiwenLiu ZhanxuWang DongmeiFan Hua - Co-evolution between viruses and autophagy has led to the emergence of viral strategies that manipulate host endoplasmic reticulum (ER) homeostasis, ultimately promoting viral replication. ER turnover is achieved through selective autophagy, also referred to as ER-phagy, which is regulated by the RETREG1/FAM134B (reticulophagy regulator 1) family of reticulon proteins. Nevertheless, how viruses target RETREG1, a receptor for ER-phagy, remains largely unclear. In this study, we demonstrate that infection with Senecavirus A (SVA), an emerging picornavirus, triggers the cleavage of RETREG1, which functions as a negative regulator of viral replication. By screening viral proteins, we identified the SVA 3C protease (3C[pro]) as the executor of this cleavage event. Detailed mapping revealed that residues Q428, E430, and G431 of RETREG1 are involved in its cleavage by the 3C[pro], and the resulting two fragments fail to suppress viral replication. Furthermore, proteolytic cleavage of RETREG1 by 3C[pro] impairs its ability to relieve ER stress and mediate ITPR1 degradation via RETREG1-dependent ER-phagy. This disruption leads to increased ER calcium (Ca) release and subsequent activation of autophagy through the CAMKK2-PRKAA2-MTOR axis, which ultimately facilitates SVA replication. Taken together, these findings indicate that SVA antagonizes the antiviral function of RETREG1-mediated ER-phagy via its 3C[pro], highlighting RETREG1 as a potential therapeutic target for combating SVA infection. 2-APB: 2-aminoethyl diphenylborinate; PRKAA2/AMPK: protein kinase AMP-activated catalytic subunit alpha 2; ATL3: atlastin GTPase 3; BHK-21: baby hamster kidney-21; CAMKK2: calcium/calmodulin dependent proteinkinase kinase2; CCPG1: cell cycle progression 1; CKAP4/CLIMP63: cytoskeleton associated protein 4; co-IP: co-immunoprecipitation; CQ: chloroquine; DAPI: 4',6-diamidino-2-phenylindole; DM: double mutant; EIF2AK3/PERK: eukaryotic translation initiation factor 2 alpha kinase 3; eGFP: enhanced green fluorescent protein; ER: endoplasmic reticulum; GFP: green fluorescent protein; HSPA5/GRP78/BiP: heat shock protein family A (Hsp70) member 5; HA: hemagglutinin; HDAC4: histone deacetylase 4; HEK-293T: human embryonic kidney 293T; hpi: hours post-infection; IFA: indirect immunofluorescence assay; ITPR1/IP3R1: inositol 1,4,5-trisphosphate receptor type 1; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; LIR: LC3-interacting region; mCherry: monomeric cherry; MTOR: mechanistic target of rapamycin kinase; REEP5: receptor accessory protein 5; RETREG1/FAM134B: reticulophagy regulator 1; RTN3: reticulon 3; SD: standard deviation; SEC61B: SEC61 translocon subunit beta; SEC62: SEC62 preprotein translocation factor; SERP1/RAMP4: stress associated endoplasmic reticulum protein 1; siRNA: small interfering RNA; SQSTM1/p62: sequestosome 1; ST: swine testis; SVA: Senecavirus A; TEM: transmission electron microscopy; TEX264: testis expressed 264, ER-phagy receptor; Tm: tunicamycin; U2OS: human osteosarcoma epithelial cells; UV: ultraviolet; ZVAD-FMK: benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone; μg: microgram; μm: micrometer; μM: micromole. - Source: PubMed
Publication date: 2026/08/11
Mao JingyuYu JuZeng PenghuiYang XiaoyuShi YongyanQu YunjieZhou JianweiWang DedongSong JiangweiWang YongLiu JueHou Lei - Poly(ADP-ribose) polymerase inhibitors (PARPi) exploit synthetic lethality in homologous recombination-deficient (HRD) cancers by trapping PARP1 on DNA, causing replication fork collapse, DNA double-strand breaks, and ultimately cell death. However, primary and acquired resistance to PARPi remains a major clinical challenge. Here, we describe a previously unrecognized mechanism for the resolution of cytotoxic trapped PARP1 through TEX264-mediated nucleophagy. We identify the p97-TEX264-nucleophagy axis as a critical pathway for the clearance of trapped PARP1 and a promising therapeutic target for overcoming PARPi resistance in HRD cancers. - Source: PubMed
Publication date: 2026/07/24
Tribble SaraRamadan Kristijan - Autophagy underlies several immunosuppressive mechanisms that collectively endow cancer cells with prominent immunoevasive features. Recent data from Hoslett et al. demonstrate that a specialized variant of autophagy commonly known as nucleophagy actively removes PARP1 molecules trapped on DNA upon pharmacological inhibition, mediating robust cytoprotective and possibly immunosuppressive effects. - Source: PubMed
Publication date: 2026/07/10
Naulin FlavieGalluzzi Lorenzo - The clinical utility of doxorubicin, a potent chemotherapeutic agent, is severely limited by its dose-dependent cardiotoxicity. Hypoxia-inducible factor 1α (HIF1α) is a key regulator of cardiovascular adaptation, but its role and mechanism in doxorubicin-induced cardiotoxicity (DIC) remain unclear. - Source: PubMed
Publication date: 2026/07/03
Wang XinyingZhan GeLi JiatianYang XinmiaoWen YuhangTang YuqiZhang PuyuXia YunlongYang Xiaolei