ATG16L1
- Known as:
- ATG16L1
- Catalog number:
- 002147A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ATG16L1
Related genes to: ATG16L1
- Gene:
- ATG16L1 NIH gene
- Name:
- autophagy related 16 like 1
- Previous symbol:
- APG16L, ATG16L
- Synonyms:
- WDR30, FLJ10035, ATG16A
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-22
- Date modifiied:
- 2015-11-24
Related products to: ATG16L1
Related articles to: ATG16L1
- During organogenesis, stem cells undergo cellular and metabolic remodelling, facilitated by autophagy-mediated turnover of organelles. Autophagy impairment has been linked to human diseases, including neurodevelopmental disorders associated with disrupted neural stem/precursor cell (NPC) homeostasis, but the underlying mechanisms and pathogenic processes governing these connections remain poorly understood. Here, we report three de novo variants of uncertain significance (p.Gly223Asp, p.Gly889Glu, p.Met978Val) in the deubiquitinase USP15 in human probands with diverse clinical features, including a spectrum of brain malformations and metabolic phenotypes. Proband variants differentially altered USP15 activity and nucleocytoplasmic localization. USP15 showed dynamic localization in NPCs of embryonic mouse cerebral cortex. Using a knock-in mouse model carrying the p.Met978Val variant, we showed that aberrant cytoplasmic accumulation of USP15, but not its loss-of-function, impaired NPC self-renewal and differentiation, leading to reduced neuronal output and enlarged lateral ventricles. Mechanistically, USP15 deubiquitinated autophagy regulator ATG16L1, impeded its normal turnover, and impaired autophagy. Concurrently, lipid droplet mobilization and mitochondrial dynamics were attenuated. Reestablishing the ubiquitination-deubiquitination balance restored autophagy activity and normal neurogenesis. Our findings suggest that nucleocytoplasmic shuttling of USP15 creates a switch-like autophagy signal controlling NPC homeostasis, and its disruption may contribute to the pathogenesis of complex neurodevelopmental conditions. - Source: PubMed
Publication date: 2026/10/06
Burns Kaylan MlZaman MashiatYoung DanielHua MichelleGao Yu-YunOr Yvonne Yan YanNobakht FarzanehWebb Bryn DJurgens Julie ARamond FrancisWei Xing-ChangRobson Caroline DPagnamenta Alistair TMegaly MarvelTafech BelalDufour AntoineShutt Timothy EAu Ping Yee BillieYang Guang - Lysosomes were once considered terminal degradative organelles responsible for disposing of cellular waste. However, recent studies have revealed that lysosomes serve as dynamic signalling and metabolic hubs at the center of diverse biological processes, including nutrient sensing, metabolic regulation, membrane trafficking, autophagy, inflammation, and cell death. To support this broad functional repertoire, lysosomes must possess robust mechanisms to maintain their integrity in the face of damage or stress. In response to lysosomal membrane damage, cells engage multilayered adaptive mechanisms that act in coordination-membrane repair (Repair), selective removal of damaged organelles (Removal), and de novo biogenesis of lysosomes (Regeneration). These processes are mediated by a range of molecular pathways, including the ESCRT complex, the PITT pathway, lysophagy, and TFEB-dependent lysosomal regeneration. Notably, recent findings highlight the noncanonical autophagy-like pathway known as ATG8ylation (conjugation of ATG8s on single membranes), which is activated via the STING-V-ATPase-ATG16L1 axis and functions as a critical hub connecting multiple arms of the lysosomal damage response. In this review, we systematically outline the molecular basis of lysosomal damage responses, including ATG8ylation, and explore how these networks are implicated in a broad spectrum of pathological conditions such as aging, neurodegeneration, cancer, obesity-related disorders, and immune dysfunction. Understanding these lysosomal quality control mechanisms not only sheds light on the fundamental principles of organelle homeostasis but also opens new avenues for therapeutic innovation. - Source: PubMed
Publication date: 2026/05/11
Minami SatoshiHamasaki Maho - Sepsis seldom presents as a uniform immune phenotype. Inflammation and immune suppression often overlap, but their balance shifts across patients, organs, and illness stages. Macrophages sit within this variation, coordinating cytokine output, microbial clearance, antigen processing, and presentation. Lipophagy removes lipid droplets through selective autophagy. The released fatty acids can feed mitochondrial β-oxidation, helping macrophages balance lipid storage with energy demand. Reduced flux may instead leave excess droplets, compromise mitochondrial function, and blunt antimicrobial activity. Whether this sequence directly drives sepsis-associated immunoparalysis remains uncertain. Protein S-palmitoylation offers a second potential control point through reversible cysteine S-acylation. Studies have linked this modification to ATG16L1 and ATG4B, and to immune regulators including MYD88, NLRP3, and CD80. Most of that evidence, however, comes from models other than sepsis, so its relevance cannot be assumed. This review therefore examines the proposed links among macrophage lipophagy, immunometabolic failure, and sepsis-associated immunoparalysis while keeping experimentally established observations separate from mechanistic inference. Taken together, current findings support S-palmitoylation as a plausible regulatory layer, but they do not establish an integrated causal axis linking S-palmitoylation, lipophagy, and immunometabolism in sepsis. This framework awaits direct testing in primary macrophages, organ-specific sepsis models, and longitudinal clinical cohorts. - Source: PubMed
Publication date: 2026/09/20
Wang YisenZhang LiangZhang LiyaoJiang HongkunCao Meiling - Parkinson's disease (PD) is characterized by dopaminergic neuron loss, α-synuclein accumulation, and sustained neuroinflammation. Autophagy can remove pathogenic α-synuclein and restrain NLR family pyrin domain containing 3 (NLRP3) inflammasome activation. Gomisin N (GN), a lignan from Schisandra chinensis, is neuroprotective, but its mechanism in PD remains incompletely defined. - Source: PubMed
Publication date: 2026/09/10
Su ChengfuDeng ZhiqiangYing Ka YeeLiu JiaGuan XinjieKan YuxuanXu XiaogangIyaswamy AshokLu KejiaLu JingWu JiaxiZhu JianguangCheung King-HoLi MinSong Juxian - Acute pancreatitis (AP) and Crohn's disease (CD) exhibit overlapping clinical presentations and an unexpectedly high rate of comorbidity. Whether this reflects shared genetic susceptibilities remains unclear. - Source: PubMed
Publication date: 2026/09/11
Xu WenbinJi AochengHan LuXiong HaoJin YiyiLin WenWu YonghuiWang YunZhong HuanXiong LongxinZeng Chunyan