ANO6
- Known as:
- ANO6
- Catalog number:
- 001672A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ANO6
Related genes to: ANO6
- Gene:
- ANO6 NIH gene
- Name:
- anoctamin 6
- Previous symbol:
- TMEM16F
- Synonyms:
- DKFZp313M0720
- Chromosome:
- 12q12
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-07
- Date modifiied:
- 2019-04-23
Related products to: ANO6
Related articles to: ANO6
- Immune checkpoint blockade (ICB) has transformed cancer therapy, yet many tumors remain refractory to treatment due to diverse immune evasion mechanisms. To uncover novel drivers of ICB resistance, we performed an in vivo CRISPR-Cas9 screen in mice with increasing levels of immune pressure. This screen identified phosphatidylserine (PS) externalization as a potent mediator of immune escape. Tumors with elevated surface PS exposure prevented reinvigoration of CD8+ T cells upon PD-1 blockade, which was associated with increased recruitment of immunosuppressive myeloid cells. Targeting of PS Synthase 1 (PTDSS1) or either of the scramblases, XKR8 or ANO6, sensitized tumors to ICB in vivo. These findings demonstrate that elevated PS exposure constitutes a mechanism of resistance to ICB, and that targeting regulators of PS externalization represents a promising strategy to enhance the efficacy of immunotherapy in refractory tumors. - Source: PubMed
Publication date: 2026/09/02
Bergholz Johann STrombley GraceCusing GwendolynLi ZhaoqiTorrence Margaret ESganga Geneva JCasey Jennifer GLiu ShangtaoChoi Ashley HMeier Samuel RKhendu TenzingYu YiTeng TengShen BinzhangStowe HannahShaaban SalamAndersen Jannik NGueroussov Serge - This study investigated genetic polymorphisms and aberrant expression of anoctamin-6 () in ankylosing spondylitis (AS) patients to clarify the role of in AS pathogenesis. - Source: PubMed
Publication date: 2026/06/29
Yang MingcanWen XianghuiWu XinyuZhang YanliGu Jieruo - TMEM16E is a transmembrane protein that functions both as a phospholipid scramblase and a non-selective ion channel, playing a critical role in cellular ion transport and membrane dynamics. Recent studies have shown that the TMEM16E scramblase also facilitates membrane internalization through macropinocytosis. This study investigates the effects of extracellular protons on TMEM16E's scrambling activity and subsequent macropinocytosis under acidic conditions, which are particularly relevant in pathophysiological contexts such as muscular dystrophies and cancers. Our results indicate that TMEM16E-induced macropinocytosis, as evidenced by the internalization of annexin V, is significantly enhanced in acidic environments (pH 5.5). However, the overall number of macropinosomes, assessed using 70 kDa dextran, remained unchanged despite variations in extracellular pH. This suggests that TMEM16E-mediated macropinocytosis operates independently of extracellular proton concentrations. Upon extracellular acidification, both TMEM16E scrambling activity and macropinocytosis were rapidly inhibited, leading to a swift decrease in intracellular Ca levels compared to physiological conditions. Notably, intracellular Ca was cleared more quickly in acidic environments, indicating a regulatory role for the proton-dependent Ca clearance pathways. Using wound healing and MTS assays, we demonstrated that TMEM16E expression significantly enhances cell proliferation and survival under acidic conditions. Our findings underscore the importance of TMEM16E-mediated macropinocytosis in maintaining plasma membrane integrity and promoting cell survival, highlighting its role as a crucial signaling pathway in both physiological and pathological contexts. - Source: PubMed
Publication date: 2026/06/16
Kim Jung-EunLee Byoung-CheolSuh Byung-Chang - To investigate the effect of β-Sitosterol on interleukin (IL)-1β-induced chondrocyte injury and the related mechanism. - Source: PubMed
Publication date: 2026/06/03
Zhang LeKong XiaochuanHong GangZheng YinfengZang Lei - TMEM63B belongs to the OSCA/TMEM63 family of mechanosensitive ion channels. We recently identified it as a mechanosensitive lipid scramblase activated by changes in membrane physical properties. Cryo-EM analysis revealed that recombinant mouse TMEM63B (mTMEM63B) protein adopts either closed or open conformations depending on the detergent environment, and that the monoclonal antibody YN9303-24 stabilizes the open state; however, the antibody epitope and the mechanism of antibody-dependent conformational regulation remained unclear. Here, using chimeric constructs, C-terminal truncations, and internal deletions, we mapped the YN9303-24 epitope to the intracellular C-terminal tail and identified the AQV motif (residues 773-775) as the core binding determinant. Functional analyses revealed that this C-terminal region is essential for maintaining TMEM63B in an inactive state under resting conditions. Deletion of the adjacent LQD motif (Δ776-778) or substitution of Leu776 with alanine induced strong constitutive lipid scrambling, evidenced by phosphatidylserine externalization and enhanced incorporation of fluorescently labeled phosphatidylcholine, whereas substitutions at Gln777 or Asp778 had minimal effects. Structural analysis positioned the AQVLQD motif adjacent to conserved intracellular helices in the open conformation, with Leu776 located near several hydrophobic residues. Together, these findings identify an autoinhibitory role for the C-terminal tail region in maintaining TMEM63B in an inactive state, suggesting that interactions between this tail and intracellular helices regulate the activity of this mechanosensitive lipid scramblase. - Source: PubMed
Publication date: 2026/06/04
Nishimura MegumiMiyata YugoShiraki YuKuribayashi RisaNomura NorimichiNishizawa TomohiroSegawa Katsumori