TOLLIP antibody - C-terminal region (ARP31758_P050)
- Known as:
- TOLLIP (anti-) - C-terminal region (ARP31758_P050)
- Catalog number:
- arp31758_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TOLLIP antibody - C-terminal region (ARP31758_P050)
Related genes to: TOLLIP antibody - C-terminal region (ARP31758_P050)
- Gene:
- TOLLIP NIH gene
- Name:
- toll interacting protein
- Previous symbol:
- -
- Synonyms:
- IL-1RAcPIP
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 2003-03-13
- Date modifiied:
- 2016-10-05
Related products to: TOLLIP antibody - C-terminal region (ARP31758_P050)
Related articles to: TOLLIP antibody - C-terminal region (ARP31758_P050)
- Selective autophagy of the endoplasmic reticulum (ER-phagy) is critical for ER proteostasis and host defense, yet how ER quality-control pathways interface with ER-phagy to restrict viral glycoproteins remains poorly defined. Previously, the 1 known ER-phagy receptor gene RETREG1 (RETR1)/FAM134B gene was reported to restrict Ebola virus (EBOV) replication in vivo by inhibiting the viral glycoprotein (GP) and viral protein 40 kDa (VP40) expression, but this mechanism remains unknown. Here, we identify the truncated RETR1/FAM134B isoform 2 (RETR1-2), but not its full-length protein RETR1, as an ER-phagy receptor that targets EBOV-GP for degradation. RETR1-2 broadly triggers GP degradation across ebolavirus species but not Marburg virus and inhibits EBOV replication. Mechanistically, RETR1-2 recognizes EBOV-GP via its luminal domain, undergoes GP-induced oligomerization, and directs GP-containing ER membranes to lysosomes through canonical macro-autophagy. Using unbiased mass spectrometry, we identified TOLLIP as the key cytoplasm adaptor for RETR1-2, which also requires cooperation with the ER chaperone calnexin for EBOV-GP degradation. Notably, the PI3P-binding C2 domain of TOLLIP mediates its interaction with RETR1-2, and the EBOV-GP degradation occurs independently of ubiquitination, revealing an unexpected role for TOLLIP in ER-phagy. Furthermore, EBOV-VP40 antagonizes this pathway by selectively targeting RETR1-2 for macroautophagic degradation independently of TOLLIP, thereby restoring GP expression and viral infectivity. Nevertheless, RETR1-2 reciprocally degrades VP40 via a similar mechanism. Together, these findings define a calnexin-TOLLIP-RETR1-2 axis that links ER quality control to ER-phagy-mediated antiviral restriction and uncover a reciprocal host-virus arms race centered on selective macro-autophagy. - Source: PubMed
Publication date: 2026/04/02
Zhang JingWang TaoWen JiaxinLan JingLi SunanZheng Yong-Hui - The clinical treatment of Osteosarcoma (OS) faces major barriers due to the risk of tumor recurrence. Immunotherapy utilizing immune checkpoint blockade (ICB) antibodies has exhibited promise in inducing tumor rejection and providing clinical benefits for patients among various tumor types. However, tumors often develop resistance to immune rejection. Given the limitations of current therapies, there is an urgent need to explore novel therapeutic strategies to enhance anti-tumor immunity and prevent recurrence. This study aims to investigate the potential of α2-adrenergic receptor (α2-AR) agonists, delivered via a thermo-sensitive hydrogel (PLGA-PEG-PLGA), as a therapeutic strategy to combat immune rejection and tumor recurrence in osteosarcoma. - Source: PubMed
Publication date: 2026/01/12
Pei Yan-HongWang ZhenZheng Yu-ShuWang Zi-YingCao Cheng-WeiLiang Hai-JieWang Bo-YangJin Zhi-JianLin Shan-YiChen Lin-XiGuo WeiXu Meng - Whether pyroptosis is controllable and reversible remains an enigma. Here we revealed that autophagy could eliminate the pore-formed N terminus of GSDME (GSDME-NT) located on membranes at different locations, suppressing pyroptosis. Crucially, GSDME-NT on the plasma membrane was eliminated through endocytic internalization, where GSDME-NT-laden vesicles were targeted and degraded as intact units. Specifically, GSDME-NT pores on the plasma membrane induced endocytosis, generating endocytosed but leaky vesicles carrying GSDME-NT. Leakage prevented acidification, necessitating further degradation through autophagy. Upon endocytosis, GSDME-NT on the vesicle membrane was labelled with ubiquitin by calcium-activated E3 ligase NEDD4L. These labelled vesicles were recognized by TOLLIP, guiding subsequent autophagosome formation, and enabling further acidification, fusion with lysosomes and eventual GSDME-NT degradation. Furthermore, in several tumour models, either disturbing autophagy or interfering with the recognition of GSDME-NT vesicles by targeting TOLLIP increased tumour cell pyroptosis, activating antitumour immunity and promoting chemotherapeutic efficacy. - Source: PubMed
Publication date: 2026/03/09
Xu ZhiminLi ZheDeng ZhenjiDing CongWu JiaweiZhang ChuqingWei HanmiaoHe TingxiangLong LiufenTang LinglongMa JunLiang Xiaoyu - As an immunosuppressive virus, the occurrence of secondary bacterial infection following porcine reproductive and respiratory syndrome virus type 2 (PRRSV-2) infection is widely recognized. The immune escape capability of PRRSV-2 enables the virus to maintain efficient proliferation even within macrophages. In this study, we report that PRRSV-2 infection disrupts the intracellular F-actin, thereby causing the inability of macrophage lysosomes to transport to secondary infected bacteria promptly for bacterial clearance. RhoA is a crucial molecule in the polymerization of G-actin to F-actin within the cell. Silencing RhoA suppresses the production of F-actin in the cell, delays the targeted clearance of bacteria by lysosomes, and leads to an increase in the number of viable bacteria within the cell. Overexpression of RhoA promotes the production of F-actin, accelerates the targeted clearance of lysosomes to bacteria, and effectively reduces the number of viable bacteria. After PRRSV-2 infection, the expression of RhoA protein is down-regulated by nsp5 to inhibit the production of F-actin. Mechanistically, nsp5 interacts with the E3 ubiquitin ligase Smurf1 to mediate K63-linked ubiquitination of RhoA at lysine 187 (K187), which subsequently leads to its degradation via the autophagy-lysosome pathway under the guidance of the selective autophagy receptor TOLLIP. Therefore, our study presents a novel mechanism through which PRRSV-2 reprograms the cytoskeleton to facilitate the survival of bacteria in secondary infections, providing a theoretical foundation and target for the prevention and control of PRRSV-2 secondary bacterial infection. - Source: PubMed
Publication date: 2026/02/27
Zheng ZifangLing XueQiao ShuangWu JieZhang ShuangquanLiu XiaoLi YangXie CaiyunMa ZhiqianGuo XuyangLi ZhiweiFeng YingtongXu LeleZhang JianwuZheng HaixueXiao Shuqi - Idiopathic pulmonary fibrosis (IPF) is a rare, chronic, progressive lung disease with high mortality and few treatment options. Using an additive genetic model, genome-wide association studies (GWAS) have identified multiple risk loci highlighting new genes and pathways of interest. Since IPF risk could also be influenced by non-additive effects, we hypothesised that association analyses using alternative genetic models may provide additional mechanistic insight. - Source: PubMed
Publication date: 2026/02/19
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