ATG9A Antibody (N-term)
- Known as:
- ATG9A Antibody (N-terminus)
- Catalog number:
- AP1814a
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ATG9A Antibody (N-term)
Related genes to: ATG9A Antibody (N-term)
- Gene:
- ATG9A NIH gene
- Name:
- autophagy related 9A
- Previous symbol:
- APG9L1
- Synonyms:
- FLJ22169
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-24
- Date modifiied:
- 2015-09-11
Related products to: ATG9A Antibody (N-term)
Related articles to: ATG9A Antibody (N-term)
- Approximately 200-300 billion cells die daily through apoptosis, a prominent form of programmed cell death, to maintain tissue homoeostasis. If apoptotic cells are not efficiently removed by phagocytes, they progress to secondary necrosis when the plasma membrane (PM) becomes permeabilised and release proinflammatory damage-associated molecular patterns (DAMPs) such as HMGB1 and ATP, which drive inflammation and contribute to autoimmune diseases. Thus, controlling inflammation through maintaining PM integrity is critical, however the molecular mechanisms underpinning this is not well defined. Here, we reveal a calcium-dependent process that delays secondary necrosis by promoting PM repair. Mechanistically, calcium influx through T-type voltage-gated calcium channels mediates the recruitment of the lipid scramblase ATG9A and Golgi components to damaged PM regions, thereby preventing early cellular lysis and DAMP release. Inhibition of calcium influx or loss of ATG9A accelerates PM rupture, increases DAMP secretion, and exacerbates inflammatory cell recruitment in vivo. Taken together, this study establishes a novel role for T-type calcium channels and ATG9A in regulating PM repair during apoptosis and highlights their therapeutic potential for controlling unwanted inflammation. - Source: PubMed
Publication date: 2026/07/08
Audi Omar FOzkocak Dilara CJohnson ChadShi BoSantavanond Jascinta PVella Caitlin LHildebrand Joanne MSharples RobynLe Quan ThinhCheng Sim LesleyBaxter Amy AHulett Mark DPoon Ivan K HPhan Thanh Kha - Non-small-cell lung cancer (NSCLC), the predominant type of lung cancer, is characterized by high invasiveness and significant mortality. Despite its clinical impact, the molecular mechanisms driving its pathogenesis and progression remain poorly understood. This study demonstrates that TMED9 is overexpressed in NSCLC and showed using multiple independent sample sets that its expression level is significantly associated with poor patient prognosis. Gain- and loss-of-function experiments revealed that TMED9 promotes proliferation, invasion, and migration of NSCLC cells in vitro and significantly accelerates tumor growth and metastasis in vivo. Mechanistically, TMED9 interacts with ATG9A and recruits USP5 to facilitate the deubiquitination and stabilization of ATG9A, thereby activating autophagy and driving malignant progression. Notably, genetic depletion of TMED9 enhances the sensitivity of NSCLC cells to osimertinib. Collectively, these findings identify the TMED9-USP5-ATG9A signaling axis as a critical driver of NSCLC malignancy, highlighting TMED9 as a promising therapeutic target. - Source: PubMed
Publication date: 2026/07/02
Liu NaHan GuohuZhang FushengGu QianhuiLiu YuanyuanJia JingZhu XiaorenChen Minbin - Parechoviruses (PeVs) are single-stranded, positive-sense RNA viruses in the family. Although most genotypes are not typically associated with severe disease, PeV-A3 has emerged as an important cause of sepsis and meningoencephalitis in newborns. Despite its clinical relevance, the life cycle and pathogenesis of PeV-A3 remain poorly understood. To identify critical host factors for PeV-A3 replication, we performed a genome-wide CRISPR screen. Our results reveal a set of Golgi-localized proteins important for viral infection, among which the lipid scramblase ATG9A (autophagy-related protein 9A) was determined to be essential across different PeV genotypes. Notably, this requirement appears to be independent of canonical autophagy. We further demonstrate that ATG9A is necessary for viral RNA replication, but not entry or translation, and co-localizes with double-stranded RNA, a marker of viral replication organelles (ROs) during infection. ATG2, a lipid transfer protein known to interact with ATG9A, is also required for optimal viral replication. Therefore, the ATG2-ATG9A complex may function by delivering key lipids into the ROs to support viral replication. - Source: PubMed
Publication date: 2026/06/26
Li YouDurnell-Bettis Lorellin AAlam FahmidaGolding Adriana EBonifacino Juan SVogt Matthew R - : Autophagy is an evolutionarily conserved intracellular degradation mechanism that is regulated by a set of autophagy-related (ATG) proteins. The only transmembrane protein among ATGs is the lipid scramblase ATG9, which exists in the form of two paralogs, ATG9A and ATG9B, in humans and other vertebrates. : Here, we analyzed human and murine skin transcriptome and proteome datasets for the expression of ATG9 paralogs and performed comparative genomics to determine their conservation during the evolution of amniotes (mammals and sauropsids). : The expression of , but not of , is enriched in differentiated epidermal keratinocytes and in skin appendages of humans and mice. In contrast to the conservation of in all major clades of amniotes, has been lost in at least three phylogenetic lineages. Cetaceans, which have unique skin adaptations to aquatic life, harbor mutations that disrupt the open reading frame of . Many or all species of turtles () and crocodilians () have entirely lost the gene. : has undergone independent pseudogenization or gene loss in different subgroups of amniotes. In mammalian species that have retained the gene, its expression pattern indicates functions of in the skin and skin appendages. - Source: PubMed
Publication date: 2026/06/09
Sukseree SupawadeeEckhart Leopold - Lens fibers undergo organelle degradation during lens terminal differentiation. Defects in organelle degradation of lens fibers lead to congenital cataract. As a member of heat shock factor family, HSF4 governs lens development by regulating the expression of key factors. HSF4 transcriptionally regulates ATG9a to induce organelle degradation via the autophagic pathway during lens terminal differentiation. HSF4 is also required for the organelle membrane translocation of phospholipases PLAATs, which were suggested to promote organelle degradation independent of autophagy in lens fibers. However, the detailed mechanism how HSF4 induces organelle degradation in lens fibers still remains unknown. In this study, we found that lipid peroxidation was extensively suppressed in HSF4 mouse lens fibers. HSF4 likely transcriptionally regulated the expression of lipoxygenase ALOX15 in lens. ALOX15 is uniquely expressed in lens fibers and colocalized with organelles in differentiating lens fibers. Knockout of ALOX15 had little effect on the organelle degradation in lens fibers. Unlike the total inhibition in HSF4 lens fibers, lipid peroxidation was only partially disturbed in ALOX15 lens fibers, possibly due to the compensatory role of ALOX12. Our findings demonstrate that HSF4 promotes lipid peroxidation by transcriptionally regulating ALOX15 expression in lens fibers, thus may contribute to the organelle degradation during lens OFZ formation. These findings expand our understanding of the molecular mechanisms underlying lens terminal differentiation. - Source: PubMed
Publication date: 2026/06/24
Zhang ShaoliWang YinanJiang NingLi XiaoyuHan LuyuanChen SiyuXie TongxinYan HongxinLi JunjieHu YanzhongMu HongmeiZhang JingCui Xiukun