Anti-Mouse SNX17 (KIAA0064), Rabbit Polyclonal
- Known as:
- Antibody toMouse SNX17 (KIAA0064), Rabbit Polyclonal
- Catalog number:
- mka0064
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Sceti
- Gene target:
- Anti-Mouse SNX17 (KIAA0064) Rabbit Polyclonal
Related genes to: Anti-Mouse SNX17 (KIAA0064), Rabbit Polyclonal
- Gene:
- SNX17 NIH gene
- Name:
- sorting nexin 17
- Previous symbol:
- -
- Synonyms:
- KIAA0064
- Chromosome:
- 2p23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-10
- Date modifiied:
- 2015-02-16
Related products to: Anti-Mouse SNX17 (KIAA0064), Rabbit Polyclonal
Related articles to: Anti-Mouse SNX17 (KIAA0064), Rabbit Polyclonal
- Recycling of internalized cell surface receptors is critical for membrane transport and receptor-mediated signaling. Formyl peptide receptor 1 (FPR1) plays important roles in host defense and inflammatory tissue injury. Here we report that fMet-Leu-Phe-Cys (fMLFC), a peptide agonist of FPR1, prevents recycling of internalized FPR1 and diverts it to the late endosome and lysosome for degradation. In contrast, FPR1 bound to the classic ligand fMLF interacts with RAB11 and SNX17, facilitating its recycling back to the cell surface. We determined a cryo-EM structure of fMLFC-bound FPR1-Gi complex. Alanine substitutions of key residues that interact with fMLFC (F102A, T177A, F178A) improved FPR1 recycling. Using a FlAsH-NanoBRET-based FPR1 biosensor, the fMLFC-induced receptor conformational change was found to be different from the fMLF-induced conformational change. fMLFC stimulation reduced FPR1 cell surface expression, along with reduced acute lung injury in LPS-treated mice. Our findings suggest that fMLFC is a chemical knockdown agent that promotes targeted protein degradation and reduces FPR1-mediated inflammation. - Source: PubMed
Publication date: 2026/03/15
Wang JunlinLiao QiwenChen GengChang YixinNie HongLu JiahongYe Richard D - Phosphatidylinositol-5-phosphate 4-kinases (PI5P4Ks) have emerged as candidate drug targets in cancer, neurological, inflammatory, and infectious diseases. Although their canonical function is to phosphorylate PI(5)P to generate PI(4,5)P, growing evidence points to additional catalytic-independent roles, but how these functions are organized within protein interaction networks remains unclear. Here, we use proximity-dependent biotin identification (BioID) in HeLa cells to map isoform-resolved interactomes of human PI5P4Kα, PI5P4Kβ, and PI5P4Kγ. This approach captures PI5P4K-proximal proteins in intact cells and reveals interaction networks positioning these kinases within trafficking-associated signaling modules. Importantly, BioID analysis indicates that PI5P4Kγ has the most extensive set of proximal interactors among the three PI5P4Ks, consistent with its comparatively low catalytic activity and a prominent scaffold-like function. Among PI5P4Kγ-enriched partners, we highlight the endosomal cargo adaptor SNX17 as a proximal interactor that links PI5P4Kγ to β1-integrin recycling and to cell migration and invasion. By providing a proximity map for all three PI5P4Ks, this study offers a framework to help define contexts in which targeted protein degradation may offer advantages over catalytic inhibition and provides a resource for future mechanistic studies on these phosphoinositide kinases. - Source: PubMed
Publication date: 2026/04/25
Llorente AliciaArora Gurpreet KLoughran Ryan MMurad RabiMaurya SvetlanaCrabtree SophiaPortillo BenjiChapagain PratimaHuluka HundaolEron ScottGoodman KristaYe GuosenBlind Raymond DEmerling Brooke M - While cisplatin is a widely used and effective chemotherapeutic agent in the treatment of head and neck squamous cell carcinoma (HNSCC), the molecular mechanisms underlying its resistance remain poorly understood. In this study, we identify OCIA domain containing 2 (OCIAD2) as a central mediator of chemoresistance and tumor progression in HNSCC. Through transcriptomic analysis and Co-immunoprecipitation coupled with mass spectrometry, we demonstrate that OCIAD2 modulates integrin signaling by directly interacting with integrin β1. Mechanistic investigations reveal that OCIAD2 does not regulate integrin β1 at the transcriptional level, but instead stabilizes its protein expression by preventing lysosomal degradation and enhancing its recycling. Importantly, OCIAD2 binds to SNX17 and enhances its association with integrin β1, promoting its recycling to lipid raft-enriched regions of the plasma membrane. By maintaining integrin β1 in these lipid raft compartments, OCIAD2 sustains the activation of the FAK-PI3K-AKT-mTOR signaling cascade, thereby fostering cellular resilience and resistance to cisplatin. Moreover, targeting OCIAD2, either through genetic silencing or RNA-based therapies, significantly sensitizes tumors to cisplatin treatment in preclinical models. This study uncovers a previously unrecognized trafficking-dependent mechanism of drug resistance, suggesting that OCIAD2 may serve as a novel therapeutic target to overcome chemoresistance in HNSCC. - Source: PubMed
Publication date: 2026/02/08
Cui LiSi ShanshanYe MinLin PeiZou MeiyanLin YunfanChen XuGuo BingSun WenjuanZhao Xinyuan - To investigate the genetic relationship between irritable bowel syndrome (IBS) and non-alcoholic fatty liver disease (NAFLD). - Source: PubMed
Publication date: 2025/12/15
Hong JundongJi RuiWang PeichengHuang FengmingZhang FanZhou YanlinLv Bin - Immune checkpoint blockade (ICB) faces limitations owing to high cost and restricted efficacy. This study identifies SNX17 as a key mediator of ICB resistance. Elevated SNX17 correlates with poor anti-PD-1 response in humans and mice. SNX17 deletion in tumor cells inhibits tumor growth via CD8 T cell-dependent mechanisms. SNX17 reduces uridine in the tumor microenvironment (TME), suppressing IFN-γ and upregulating PD1 in CD8 T cells. Exogenous uridine shows antitumor efficacy comparable to anti-PD-1/PD-L1 in low-SNX17 tumors and overcomes resistance in high-SNX17 models. Uridine enhances CD8 T cell function by promoting CD45 N-glycosylation and LCK phosphorylation. Mechanistically, SNX17 stabilizes RUNX2, promoting UPP1 transcription and uridine degradation in the TME. These findings position SNX17 as an ICB response biomarker and nominate uridine as a cost-effective immunotherapeutic strategy. - Source: PubMed
Publication date: 2025/12/29
Xiao JianbiaoLi ZhiyangDing YiZhu KejinZheng ZhihaoZhang YaoweiWeng JiawenWang FeifeiZhang YuqinZeng SisiQiu MinxingZhang ZhaowenWang ZhizhangLiang Li