ABHD10
- Known as:
- ABHD10
- Catalog number:
- GTX119172
- Product Quantity:
- 0.1 ml
- Category:
- -
- Supplier:
- ACR
- Gene target:
- ABHD10
Related genes to: ABHD10
- Gene:
- ABHD10 NIH gene
- Name:
- abhydrolase domain containing 10
- Previous symbol:
- -
- Synonyms:
- FLJ11342
- Chromosome:
- 3q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-24
- Date modifiied:
- 2012-03-26
Related products to: ABHD10
Related articles to: ABHD10
- Palmitoylation is the only fully reversible post-translational lipid modification that impacts 10-20% of the human proteome, but its role during spermatogenesis remains enigmatic. In this study, through generating HA-tagged Abhd10 knock-in mice, Abhd10-null mice, and combining super-resolution fluorescence imaging and electron microscopy, we identify that the S-depalmitoylase ABHD10 (abhydrolase domain containing 10) is a mitochondrial matrix protein, specifically expressed in testis and is essential for male fertility. Abhd10 knockout mice manifest severe sperm motility defects accompanied by malformed mitochondrial sheaths of sperm. Mitochondrial proteomic analysis reveals that ABHD10 deficiency downregulates respiratory chain complex proteins and mitochondrial sheath formation factors SPATA19 and GK2. Using mass spectrometry-based mitochondrial acyl-biotin exchange assays, we systematically identify that loss of ABHD10 leads to the hyper-palmitoylation of multiple functionally critical proteins, including mitochondrial sheath formation factors (SPATA19 and GK2) and aerobic respiration regulators (PDHX, NDUFV1 and SDHB). Co-immunoprecipitation and proximity labeling assays reveal the physical interactions between ABHD10 and its substrates (SPATA19, GK2, PDHX). Collectively, ABHD10 may bind to and mediate the S-depalmitoylation of SPATA19, GK2, and PDHX, thereby regulating the formation of the sperm mitochondrial sheath and mitochondrial function. This work not only identifies S-depalmitoylase ABHD10 as a key determinant of male fertility but also advances our understanding of post-translational regulation during spermatogenesis. - Source: PubMed
Publication date: 2025/11/24
Zhou ShuminZhou HaoXu HaoranXiong MengnengGan ShimingLiu DalinZhao YifanYu ZiqiLuo ChunhaiZhang YujunZhang BeibeiSun Fei - Cardiac conduction disorders predispose individuals to arrhythmias, currently but the exact mechanisms of cardiac conduction remain elusive. The study sought to identify the causal association between circulating plasma proteins and electrocardiogram (ECG) traits, offer valuable biological insights and clinical guidance into cardiac conduction. - Source: PubMed
Publication date: 2024/10/31
Zhao PengMeng LiHan FeiyuanYu ZhongzhiWang YidanWu YunfeiWang YanYu BoLiu XinxinTian Jinwei - Alcoholic liver disease (ALD) and other forms of chronic hepatotoxic injury can lead to transforming growth factor β1 (TGFβ1)-induced hepatic fibrosis and compromised liver function, underscoring the need to develop novel treatments for these conditions. Herein, our analyses of liver tissue samples from severe alcoholic hepatitis (SAH) patients and two murine models of ALD reveals that the ALD phenotype was associated with upregulation of the transcription factor ETS domain-containing protein (ELK-3) and ELK-3 signaling activity coupled with downregulation of α/β hydrolase domain containing 10 (ABHD10) and upregulation of deactivating S-palmitoylation of the antioxidant protein Peroxiredoxin 5 (PRDX5). In vitro, we further demonstrate that ELK-3 can directly bind to the ABHD10 promoter to inhibit its transactivation. TGFβ1 and epidermal growth factor (EGF) signaling induce ABHD10 downregulation and PRDX5 S-palmitoylation via ELK-3. This ELK-3-mediated ABHD10 downregulation drives oxidative stress and disrupts mature hepatocyte function via enhancing S-palmitoylation of PRDX5's Cys100 residue. In vivo, ectopic Abhd10 overexpression ameliorates liver damage in ALD model mice. Overall, these data suggest that the therapeutic targeting of the ABHD10-PRDX5 axis may represent a viable approach to treating ALD and other forms of hepatotoxicity. - Source: PubMed
Publication date: 2023/07/03
Li Tian-ZhuBai Chun-YingWu BaoZhang Cong-Ying Wang Wen-TaoShi Tie-WeiZhou Jing - Recently, microRNAs (miRNAs), have been extensively investigated in diseases. The upregulated expression of miR-19b-3p has been validated in patients with hypertrophic cardiomyopathy. Nonetheless, it regulatory mechanism in myocardial infarction (MI) is still unclear. - Source: PubMed
Publication date: 2022/08/18
Liao BihongDong ShaohongXu ZhengleiGao FeiZhang SuihaoLiang Ruijuan - S-Palmitoylation is a reversible lipid post-translational modification that has been observed on mitochondrial proteins, but both the regulation and functional consequences of mitochondrial S-palmitoylation are poorly understood. Here, we show that perturbing the 'erasers' of S-palmitoylation, acyl protein thioesterases (APTs), with either pan-active inhibitors or a mitochondrial-targeted APT inhibitor, diminishes the antioxidant buffering capacity of mitochondria. Surprisingly, this effect was not mediated by the only known mitochondrial APT, but rather by a resident mitochondrial protein with no known endogenous function, ABHD10. We show that ABHD10 is a member of the APT family of regulatory proteins and identify peroxiredoxin-5 (PRDX5), a key antioxidant protein, as a target of ABHD10 S-depalmitoylase activity. We then find that ABHD10 regulates the S-palmitoylation status of the nucleophilic active site residue of PRDX5, providing a direct mechanistic connection between ABHD10-mediated S-depalmitoylation of PRDX5 and its antioxidant capacity. - Source: PubMed
Publication date: 2019/11/18
Cao YangQiu TianKathayat Rahul SAzizi Saara-AnneThorne Anneke KAhn DanielFukata YukoFukata MasakiRice Phoebe ADickinson Bryan C