TGOLN2 Antibody (OASA09276)
- Known as:
- TGOLN2 Antibody (OASA09276)
- Catalog number:
- oasa09276
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TGOLN2 Antibody (OASA09276)
Related genes to: TGOLN2 Antibody (OASA09276)
- Gene:
- TGOLN2 NIH gene
- Name:
- trans-golgi network protein 2
- Previous symbol:
- -
- Synonyms:
- TGN51, TGN46, TGN48, TGN38, TTGN2
- Chromosome:
- 2p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-08-07
- Date modifiied:
- 2014-11-19
Related products to: TGOLN2 Antibody (OASA09276)
Related articles to: TGOLN2 Antibody (OASA09276)
- WNT2B is canonically characterized as a secreted WNT-family ligand, which is transported to the extracellular space via the endoplasmic reticulum (ER)-Golgi pathway and binds to cell surface FZDs (frizzled class receptors) to trigger downstream signaling cascades. Here, we identify a previously unrecognized non-secretory intracellular function of WNT2B in impairing endosomal trafficking to inhibit macroautophagy/autophagy, as well as a non-canonical LC3B-II-dependent autophagic secretion mechanism for WNT2B. Specifically, the non-secretory intracellular pool of WNT2B via its conserved middle domain (MD) binds to the spectrin repeat domain (SRD) of WASHC5, competitively displacing WASHC1 and thereby disrupting WASH complex assembly and inhibiting WASHC1-mediated actin polymerization on early endosomes. This disruption impairs endosomal cargo trafficking, including the core autophagy protein ATG9A, leading to defective autophagy initiation and subsequent accumulation of pro-inflammatory and pro-fibrotic factors in fibroblasts. We validated this mechanism in vivo using a TNBS-induced mouse model of chronic colitis. Fibroblast-specific deletion restores autophagy, reduces pro-inflammatory cytokine secretion, and ameliorates intestinal fibrosis. Consistently, in Crohn disease (CD) patient tissues, elevated WNT2B in fibrotic regions negatively correlates with autophagy activity, and positively correlates with pro-fibrotic phenotypes, and clinical disease severity. Moreover, we identify a novel LC3B-II-dependent autophagic secretion pathway for WNT2B, which is distinct from the conventional ER-to-Golgi-dependent protein secretion. Collectively, our study delineates a novel non-canonical WNT2B-WASH complex-ATG9A regulatory axis through which WNT2B impairs endosomal trafficking and disrupts autophagy, ultimately amplifying inflammation and fibrosis. This study suggests that WNT2B may serve as a promising therapeutic target for CD and autophagy-associated fibrotic disorders.: 3-MA: 3-methyladenine; AAV: adeno-associated virus; ACTA2: actin alpha 2, smooth muscle; ARPC2: actin related protein 2/3 complex subunit 2; ATG: autophagy related; CCN3: cellular communication network factor 3; CD: Crohn disease; CK666: 2-fluoro-N-[2-(2-methyl-1H-indol-3-yl)ethyl]benzamide; COL1A1: collagen type I alpha 1 chain; Co-IP: co-immunoprecipitation; CTNNB1: catenin beta 1; DBcAMP: dibutyryl cyclic adenosine monophosphate; DPT: dermatopontin; EEA1: early endosome antigen 1; EGFR: epidermal growth factor receptor; ELISA: enzyme-linked immunosorbent assay; ER: endoplasmic reticulum; ESCRT: endosomal sorting complexes required for transport; EV: extracellular vesicle; FRAP: fluorescence recovery after photobleaching; FL: full length; FZD: frizzled class receptor; GST: glutathione S-transferase; HIF: human intestinal fibroblast; HMGB1: high mobility group box 1; IKBKB: inhibitor of nuclear factor kappa B kinase subunit beta; IL6: interleukin 6; LDELS: LC3-dependent EV loading and secretion; LPS: lipopolysaccharide; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MD: middle domain; MEFs: mouse embryonic fibroblasts; MTOR: mechanistic target of rapamycin kinase; MVB: multivesicular body; NFKB: nuclear factor kappa B; NFKBIA: NFKB inhibitor alpha; PDCD6IP: programmed cell death 6 interacting protein; PLA: proximity ligation assay; RELA/p65: RELA proto-oncogene, NF-kB subunit; SAFB: scaffold attachment factor B; SES-CD: Simple Endoscopic Score for Crohn disease; SIM: super-resolution structured illumination microscopy; SMAD3: SMAD family member 3; SQSTM1/p62: sequestosome 1; SRD: spectrin repeat domain; TEM: transmission electron microscopy; TFRC: transferrin receptor; TGFB1: transforming growth factor beta 1; TGOLN2: trans-golgi network protein 2; TNBS: 2,4,6-trinitrobenzenesulfonic acid; TNF: tumor necrosis factor; VCA: Verprolin homology, Central and Acidic; WASHC: WASH complex subunit; WLS: Wnt ligand secretion mediator; WCL: whole cell lysates; WNT: Wnt family member; WT, wild type. - Source: PubMed
Publication date: 2026/06/03
Liu DanqiongCheng YanlingHuang ChuxiangXie KangJie JiananZhang QingqingLan LinChen PeiyuXie JingWang HongliRen LuLi HuiwenGeng LanlanGong SitangZhu YunCheng Yang - Immunotherapy has improved survival across multiple malignancies but remains largely ineffective in solid cancers such as lung, breast, and pancreatic cancer. A key driver of resistance is the immunosuppressive tumor microenvironment (TME). Although numerous mediators of TME immunosuppression have been identified, therapeutic targeting has provided limited clinical benefit. Tumor-derived extracellular vesicles (EVs) have recently emerged as contributors to resistance, yet their mechanisms remain unclear. We developed human non-small cell lung cancer models to investigate EV-mediated immunosuppression. We identified a distinct Golgi-derived EV subpopulation that potently suppress T cell function and tumor infiltration. These EVs express the -Golgi network marker TGOLN2, and exhibit minimal levels of canonical EV markers. TGOLN2 overexpression drives this suppressive phenotype. Clinically, elevated associates with poor survival and correlate with an immunosuppressive TME signature across more than 20 cancer types, including NSCLC. Collectively, this work defines a previously unrecognized mechanism of TGOLN2-driven, EV-mediated immunosuppression. - Source: PubMed
Publication date: 2026/05/13
Sohal Ikjot SShaw Sydney NDos Santos Andrea PElzey Bennett DHarper Haley AnneMcMahan CarliMeeks Lauren NHasan HumnaSoto-Vargas ZulaidaAbdullah NoorSahoo Subhransu SekharKazemian MajidOlson Matthew RKasinski Andrea L - The term CASM describes a process in which MAP1LC3B/LC3B and other Atg8-family proteins are covalently ligated to lipids in damaged endomembranes. While CASM is commonly described as a cytoprotective response to multiple types of membrane damage, how CASM helps cells maintain homeostasis is still unclear. Here, we show that CASM maintains Golgi apparatus architecture following the loss of TRIM46, a ubiquitin ligase with roles in microtubule organization. TRIM46 deficient cells were notable for enhanced TFEB-driven lysosomal biogenesis and Golgi ribbon fragmentation, with colocalization of the -Golgi marker TGOLN2 and the Atg8-family proteins LC3B and GABARAP. Further studies revealed that the Golgi Atg8ylation seen in knockout cells was not degradative and mechanistically resembled CASM. Genetic inhibition of CASM in TRIM46 deficient cells reduced TFEB activation and exacerbated the Golgi morphology defects, suggesting that CASM contributes to Golgi repair. Accordingly, Golgi reformation after drug-induced fragmentation was impaired upon knockdown of CASM genes. Together, these studies identify lysosomal biogenesis and CASM as coordinated features of a Golgi damage response, with CASM acting to preserve Golgi integrity. AMPK (AMP-activated protein kinase); ATG3 (autophagy related 3); ATG5 (autophagy related 5); ATG7 (autophagy related 7); ATG12 (autophagy related 12); ATG13 (autophagy related 13); ATG16L1 (autophagy related 16 like 1); BECN1 (beclin 1); CASM, conjugation of Atg8 to single membranes; GABARAP (GABA type A receptor-associated protein); GABARAPL1 (GABA type A receptor associated protein like 1); GABARAPL2 (GABA type A receptor associated protein like 2); GOLGA2 (golgin A2); HT (HaloTag); HL (HaloTag ligand); MAP1LC3A/LC3A (microtubule associated protein 1 light chain 3 alpha); MAP1LC3B/LC3B (microtubule associated protein 1 light chain 3 beta); MAP1LC3C/LC3C (microtubule associated protein 1 light chain 3 gamma); MTORC1 (mechanistic target of rapamycin kinase complex 1); PE (phosphatidylethanolamine); PIK3C3/VPS34 (phosphatidylinositol 3-kinase catalytic subunit type 3); PS (phosphatidylserine); TECPR1 (tectonin beta-propellor repeat containing 1); SQSTM1/p62 (sequestosome 1); TFEB (transcription factor EB); TFE3 (transcription factor binding to IGHM enhancer 3); TGOLN2 (trans-golgi network protein 2); TRIM46 (tripartite motif containing 46); ULK1 (unc-51 like autophagy activating kinase 1); ULK2 (unc-51 like autophagy activating kinase 2): VAIL (V-ATPase-ATG16L1 induced LC3 lipidation). - Source: PubMed
Publication date: 2026/05/18
Oh SeeunUllah SaifSaha BhaskarMandell Michael A - The lysosome is not only a degradative organelle but also an essential platform for signal transduction, such as with MTOR signaling. The reciprocal regulation between the lysosome and MTOR is central to macroautophagy/autophagy and metabolism. MTOR-mediated suppression of lysosomal acidification is important for lysosomal activity, autophagic flux, and cell survival. VASN is a transmembrane glycoprotein whose function is not fully understood. In the present study, we report that VASN is a TGFB-inducible protein and plays a crucial role in positively regulating lysosomal acidification. As a potential mechanism, we demonstrated that VASN localizes to the lysosome, interacts with lysosomal MTOR and STK11IP, and disrupts the binding of STK11IP to MTOR and the V-ATPase, which was recently reported to suppress lysosomal acidification. We found that VASN's function in modulating lysosomal activity is essential for optimal mitophagy induced by TGFB and terminal erythroid differentiation and is critical for the progression of mutant KRAS-driven lung cancer. Overall, our study identified VASN as a novel TGFB-inducible regulator of lysosomal function.: ATG5, autophagy related 5; BNIP3, BCL2 interacting protein 3; BNIP3L, BCL2 interacting protein 3 like; CLEM, correlative-light electron microscopy; DSP, dithiobis(succinimidyl propionate); EGFP, enhanced green fluorescent protein; EYFP, enhanced yellow fluorescent protein; FIB-SEM, focused ion beam-scanning electron microscopy; LAMP1, lysosomal-associated membrane protein 1; LysoIP, lysosomal immunoprecipitation; MAP1LC3B, microtubule-associated protein 1 light chain 3 beta; MTOR, mechanistic target of rapamycin kinase; RBCs, red blood cells; SMAD, SMAD family member; STK11IP, serine/threonine kinase 11 interacting protein; TEM, transmission electron microscopy; TGFB, transforming growth factor beta; TGOLN2/TGN38, trans-golgi network protein 2; TMEM192, transmembrane protein 192; V-ATPase, vacuolar-type H-translocating ATPase. - Source: PubMed
Publication date: 2026/02/15
Yan JiongZhang YanChoksi SwatiMikolaj Melissa RHarned AdamNarayan KedarLiu Zheng-Gang - The interaction between HIV-1 and host immune cells, particularly macrophages, is crucial in understanding viral persistence and pathogenesis. This study aims to explore the impact of HIV-1 infection on macrophage microRNA (miRNA) expression profiles using a systems biology approach to uncover the potential role of miRNAs in modulating macrophage functionality and identify key miRNA targets that may serve as therapeutic avenues. - Source: PubMed
Publication date: 2025/05/01
Harshithkumar RKaul MollinaChandane-Tak MadhuriSiddiqi Nikhat JMalik AbdulKhan Abdul ArifMukherjee Anupam