ATG4B
- Known as:
- ATG4B
- Catalog number:
- 002137A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ATG4B
Related genes to: ATG4B
- Gene:
- ATG4B NIH gene
- Name:
- autophagy related 4B cysteine peptidase
- Previous symbol:
- APG4B
- Synonyms:
- Apg4B, KIAA0943, DKFZp586D1822, AUTL1
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-23
- Date modifiied:
- 2016-02-23
Related products to: ATG4B
Related articles to: ATG4B
- Programmed death-ligand 1 (PD-L1) undergoes continuous endocytosis and post-endocytic sorting that determine its recycling to the plasma membrane, lysosomal degradation, and exosomal secretion. Although PD-L1 internalization depends on RAB5-mediated endocytosis, whether canonical autophagy contributes to the subsequent sorting of internalized PD-L1 remains unclear. Here, we show that canonical autophagy is dispensable for the post-endocytic fate of cell-surface PD-L1. Genetic disruption of core autophagy components, including LC3B, ATG4B, ATG5, and ATG7, did not impair delivery of internalized PD-L1 to early endosomes, multivesicular bodies (MVBs), late endosomes, or extracellular vesicles. Pharmacologic inhibition of autophagosome-lysosome fusion increased PD-L1 accumulation in RAB5- and CD63-positive compartments, but this effect persisted in cells lacking LC3B, ATG5, or ATG7, further indicating that canonical autophagy is not required for PD-L1 endosomal sorting or exosomal secretion. Instead, we identify CAPZ, a CAPZα-CAPZβ heterodimer best known for actin filament capping, as a regulator of PD-L1 post-endocytic sorting. Loss of CAPZ reduced PD-L1 delivery to CD63-positive MVBs and incorporation into exosomes while increasing its accumulation in RAB11-positive recycling endosomes, resulting in elevated cell-surface PD-L1. Functionally, CAPZ-deficient tumor cells were less sensitive to peripheral blood mononuclear cell-mediated killing, consistent with increased surface PD-L1 and enhanced immune-evasive capacity. Together, these findings indicate that CAPZ-dependent endosomal maturation controls the balance between PD-L1 recycling and MVB/exosomal sorting independently of canonical autophagy, thereby influencing PD-L1 surface abundance and tumor immune evasion. - Source: PubMed
Publication date: 2026/09/29
Xu PengYe ZuodongZhu YanniChan Chuen-FukLi YanhuaHuang HuiruZhu ChengyiZhang XiaoyinWang YijingWang YilinLin NaixinSun WeiPeng MeiyuLu YingyingYue Jianbo - 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 - [This corrects the article DOI: 10.1016/j.bbrep.2025.102418.]. - Source: PubMed
Publication date: 2026/08/17
Afzali Fereshteh MohebHeshmati MasoumehSalimi AliKalanaky SomayehFakharzadeh SaidehHafizi MaryamAkbari Mohammad EsmailNazaran Mohammad HassanHashemi Mehrdad - - Source: PubMed
Publication date: 2026/08/26
Chi RuifangShi FangHe JuanCai YanLv MengzhuCao HuiliChai ChanjuanZhao YanfangYang BingCui Xuelin - Excessive vascular smooth muscle cell (VSMC) proliferation/survival is a critical event underlying restenosis and vascular remodeling. Tripartite motif-containing 24 (TRIM24) is an oncogenic TRIM family protein with E3 ubiquitin ligase and transcriptional co-regulator functions. This study aimed to elucidate the critical role of TRIM24 in modulating VSMC functions and neointimal hyperplasia. - Source: PubMed
Publication date: 2026/07/29
Singh MonikaSarkar AnkanZargar Zahid BashirMukheja YashdeepPawar Sandip VChopra KanwaljitJain Manish