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)
- 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 - The fungal plasma membrane is the target of fungicidal compounds, such as polyenes and saponins, that directly interact with fungus-specific ergosterol to cause deleterious membrane disruption. To counter membrane attack, diverse eukaryotic cells employ Ca2+-binding penta-EF (PEF)-hand proteins, including the human ortholog, ALG-2, to maintain membrane integrity. Candida albicans is a major fungal pathogen in humans, where increasing resistance to current antifungal drugs that target the plasma membrane is of serious concern. Combinatorial treatments that additionally compromise the plasma membrane offer a way forward, but our mechanistic understanding of how fungi respond to direct membrane disruption remains limited. Here, we investigated the PEF-hand ortholog, Pef1, in this polymorphic species. GFP-tagged Pef1 localized at sites of polarized growth in yeast and hyphal cells of C. albicans. On treatment of hyphae with the polyene drug, amphotericin B, or the saponin tomatine, GFP-Pef1 became distributed as punctate spots at the membrane. In a similar manner, loss of calcineurin A (Cna1), but not of its transcription factor, Crz1, caused this punctate localization pattern of GFP-Pef1. While deletion of PEF1 slightly impaired yeast cell growth rate, filamentation was not affected. Strikingly, pef1Δ hyphae could not maintain plasma membrane integrity in serum, as also seen in the cna1Δ mutant, and exhibited attenuated virulence in an insect larvae infection model. Together, these observations suggest that Pef1 localizes to sites of membrane perturbation in order to maintain cell integrity, including sites of dynamic polarized growth, septum formation, and fungicide-induced membrane disruption. - Source: PubMed
Publication date: 2026/04/01
Weichert MartinSchumann Marcel RenéBrandt UlrikeBedford CameronBrand Alexandra CFleißner André - Endoplasmic reticulum (ER) exit sites (ERES) serve as essential hubs for the packaging and export of secretory proteins into the COPII vesicular pathway. Previous studies have shown that ERES are dynamic and capable of adapting to stress, but the molecular details controlling their degradation under nutrient-stress conditions were largely unknown. A recent study by Liao et al. introduces a new mechanism in which ERES are degraded through lysosome-dependent microautophagy in response to nutrient stress. This process is uniquely facilitated by COPII components, the calcium-binding adaptor ALG2, and the ESCRT machinery. The authors demonstrate that inhibiting MTOR triggers calcium release from lysosomes, which then recruits ALG2, leading to SEC31 ubiquitination and subsequently promoting PDCD6IP/ALIX-ESCRT-dependent lysosomal engulfment of ERES. This research reveals an unexplored pathway for the quality control and recycling of secretory machinery, thereby improving our understanding of ER turnover and establishing a mechanistic link between nutrient sensing, autophagy, and remodeling of the secretory pathway. - Source: PubMed
Publication date: 2026/02/23
Bhattacharyya DibyenduKlionsky Daniel J - Congenital disorders of glycosylation (CDG) are a complex and heterogeneous family of rare metabolic diseases that affect protein and lipid glycosylation and glycosylphosphatidylinositol synthesis. These disorders can affect multiple organs, leading to a broad spectrum of symptoms that vary among different CDG subtypes and between individuals with same type of CDG. This study aimed to investigate the genetic variants, molecular etiologies, and clinical features of 20 Chinese patients diagnosed with CDG. - Source: PubMed
Publication date: 2025/12/23
Zhao PeiweiTan LiMeng QingjieZhang LeiHuang YufengZhang XiankaiHu YanqiuZhou ShiqiongHe Xuelian - Glycosylation defects are a recognized cause of congenital myasthenic syndrome (CMS), affecting the stability and functions of the neuromuscular junction proteins. Mutations in five genes (GFPT1, DPAGT1, GMPPB, ALG2, and ALG14) are currently associated with glycosylation-related CMS. This cohort describes Iranian patients with CMS and variants in these genes. - Source: PubMed
Publication date: 2025/11/28
Ramezani MahtabOkhovat Ali AsgharNilipour YaldaGhasemi AidaAshtiani Bahram HaghiSarraf PayamKariminejad ArianaNafissi Shahriar