ALG2 Antibody (Center)
- Known as:
- ALG2 Antibody (Center)
- Catalog number:
- AP17233c
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ALG2 Antibody (Center)
Related genes to: ALG2 Antibody (Center)
- Gene:
- ALG2 NIH gene
- Name:
- ALG2 alpha-1,3/1,6-mannosyltransferase
- Previous symbol:
- -
- Synonyms:
- CDGIi, FLJ14511, hALPG2, NET38, CDG1I
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-15
- Date modifiied:
- 2019-01-18
Related products to: ALG2 Antibody (Center)
Related articles to: ALG2 Antibody (Center)
- The endosomal sorting complex required for transport (ESCRT) is a hetero-multimeric membrane-remodeling machinery essential for endosomal sorting, intraluminal vesicle formation, cytokinetic abscission, and membrane repair. ESCRT is also hijacked by some pathogens including the protozoan , which subverts it at the parasitophorous vacuole membrane to support parasite ingestion of host cytosolic proteins. Although the ESCRT accessory protein, ALG-2 is recruited to the parasitophorous vacuole, nothing was known about how this happens. Herein we identify the dense granule protein TgGRA8 as a key effector that recruits ALG-2 and ALIX to the parasitophorous vacuole. We show that TgGRA8 directly binds ALG-2 via conserved ALG-2-binding elements like those found in other ALG-2 interacting proteins including ALIX and SEC31A. Biochemical assays show high-affinity, Ca-dependent TgGRA8-ALG-2 binding, and structural modeling suggests TgGRA8 may assemble multivalently to coordinate multiple ALG-2 dimers, stabilizing ALG-2/ALIX recruitment through a non-canonical bridging mechanism. Conservation of these motifs among tissue cyst-forming coccidians implies a lineage-linked adaptation that supports infection by these parasites. Metabolomics further indicates that TgGRA8 loss disrupts amino acid, purine, and central carbon metabolism, like those seen in other ingestion deficient mutants. Together, these findings uncover a conserved, multivalent strategy by which engages host ALG-2 to organize ESCRT at the parasitophorous vacuole, thereby coupling nutrient acquisition to metabolic fitness and exposing a novel agent for probing ESCRT biology. - Source: PubMed
Publication date: 2026/07/20
Kaur HargobinderGuevara Rebekah BRivera-Cuevas YolandaOlafsson Einar BMayoral JoshuaAugusto LeonardoGuerra Alfredo JPatel RomirBohannon Kevin PSexton Jonathan ZHanson Phyllis IWeiss Louis MCarruthers Vern B - The prion-like spread of tau from cell to cell in the central nervous system involves escape from the endolysosomal network, which is counteracted by the lysosomal repair activity of the ESCRT system. Here, we investigate whether other components of the lysosomal damage sensing and repair system, namely the ESCRT-recruiting Ca sensor ALG-2, conjugation of ATG8s to single membranes (CASM), the phosphoinositide-initiated tethering and lipid transport (PITT) pathway, and the Parkinson's disease-related lipid transporter VPS13C are involved in tau spread. We found that the PITT pathway and VPS13C are strongly implicated in tau seeding by pre-formed fibrils (PFFs) in both neurons and astrocytes, CASM has a major role in astrocytes but not neurons, and ALG-2 has a lesser role in both. We then investigated the mechanism of damage and seeding by tau PFFs using cryo-electron tomography. Unlike the classical lysosome damage agent LLOMe, tau PFFs were not seen to directly interact with the lysosomal membrane, nor do they distort local membrane curvature. Lysosomes in PFF-treated cells were structurally intact. Extensive protein aggregates of similar character were seen in both the lysosomal lumen and in the cytosol proximal to lysosomes. The observations are consistent with the PFF-induced co-aggregation of tau with other cellular materials within lysosomes, with leakage to the cytosol attributed to reversible holes in the lysosome membrane. - Source: PubMed
Publication date: 2026/06/10
Herrmann EricTan ShuixiaRose Kevin MHooy Richard MHurley James H - Tumor cells are constantly confronted with nutrient deprivation; however, the effect of serum starvation on the remodeling of endosomal compartments and extracellular vesicles (EVs) in tumor cells remains unclear. Here, we found that serum starvation pronouncedly promotes multivesicular body (MVB) biogenesis, EV formation, and cargo selection. Specifically, by generating a constitutively active Rab5Q79L mutant to induce the enlargement of MVB, we revealed for the first time to our knowledge that ANXA3 is sorted into intraluminal vesicles (ILVs) of MVB. Mechanistically, we confirmed that serum starvation regulates the endosomal sorting complex required for transport-associated (ESCRT-associated) protein ALG-2 interacting protein X (ALIX), which recruits ESCRT-III to MVB and binds to annexin A3 (ANXA3) to mediate its sorting into ILVs of MVB. Our study highlights that serum starvation promotes an ALIX-dependent ESCRT-III recruitment pathway, which loads protumor ANXA3 cargo to exert a profound effect on tumor progression. - Source: PubMed
Publication date: 2026/06/08
Peng XueqiangLiu JiaxingZeng GuolongXiao YafeiHao ZhixiongHe GuangpengJin HongyuanGao YuTang ShileiWei ShiboLi YanYu YifanYang LiangLi Hangyu - (Turcz.) Baill. (Schisandraceae) is a medicinal plant widely distributed in East Asia and has long been used in traditional herbal medicine. Phytochemical studies have identified lignans as the major bioactive constituents of , among which Schisandrin B (Sch B) is one of the most abundant and pharmacologically active compounds. Previous studies have demonstrated that Sch B exhibits a variety of biological activities, including antioxidant, anti-inflammatory, hepatoprotective, and cytoprotective effects. As a natural lignan compound derived from , Sch B has attracted increasing attention for its potential protective effects against environmental and inflammatory insults. This study aimed to investigate the protective effects of Sch B against PM-induced inflammatory injury in THP-1 cells and to elucidate the underlying molecular mechanisms. An in vitro PM-induced THP-1 cell injury model was established by stimulating THP-1 cells with PM. Subsequently, Sch B was applied to the model, and inflammation-related indicators and pathways were detected using methods such as ELISA, PCR, and Western Blot (WB). The results showed that Sch B significantly inhibited interleukin-1β (IL-1β) secretion and attenuated PM-induced pyroptosis in THP-1 cells. Mechanistically, Sch B alleviated cell membrane damage and inflammatory factor release by suppressing Caspase-1 activation and inhibiting the cleavage of gasdermin D (GSDMD) into its active N-terminal fragment (N-GSDMD). Furthermore, Sch B treatment was associated with the up-regulation of ALG-2, ALIX, and TSG101, suggesting the potential involvement of ESCRT-III-associated membrane repair mechanisms. In conclusion, Sch B, a natural lignan compound derived from , exhibits protective effects against PM-induced THP-1 cell pyroptosis by reducing cell membrane damage and inflammatory cytokine release. These effects are associated with the inhibition of Caspase-1 activity and GSDMD cleavage, as well as the activation of ESCRT-III-associated membrane repair responses. Collectively, these findings highlight the potential of Sch B as a natural cytoprotective compound against particulate matter-induced inflammatory injury. - Source: PubMed
Publication date: 2026/05/09
Deng LeLiao Lian-YingLing XiaoLi LiHe You-JieGuo Miao-Miao - N-glycosylation in eukaryotes begins with the assembly of a lipid-linked oligosaccharide on the endoplasmic reticulum membrane. As a pivotal post-translational protein modification, it is conserved across all three domains of life. However, the evolutionary origins of the Nglycosylation pathway remain a subject of ongoing debate in evolutionary biology, largely due to the limited availability of robust data regarding the evolutionary trajectories of the glycosyltransferases involved in this process. Here, we present phylogenetic analyses of the eukaryotic ALG1 and ALG2 mannosyltransferases (MTases), which are crucial for constructing the core trimannosyl Man3GlcNAc2 structure conserved in eukaryotic N-glycans. Our comprehensive phylogenetic study, combined with functional and structural analyses, suggests that the ALG2 MTase likely originated from a bacterial ancestor. This inference is further supported by the identification of sequential and functional ALG1 homologs exclusively within bacterial lineages, rather than in Asgard archaea or other archaeal groups. Our findings challenge the prevailing hypothesis that the eukaryotic N-glycosylation pathway primarily evolved from archaeal ancestors, instead suggesting a chimeric origin involving contributions from both bacterial and archaeal lineages. - Source: PubMed
Xu SiChen ShuaiGu Yu-HeHuang Yi-FanNakanishi HidekiGao Xiao-Dong