Ask about this productRelated genes to: USP30 Blocking Peptide
- Gene:
- USP30 NIH gene
- Name:
- ubiquitin specific peptidase 30
- Previous symbol:
- -
- Synonyms:
- MGC10702, FLJ40511
- Chromosome:
- 12q24.11
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-30
- Date modifiied:
- 2016-10-05
Related products to: USP30 Blocking Peptide
Related articles to: USP30 Blocking Peptide
- Alveolar Type II cells (AT2s) are the stem cells responsible for both lung homeostasis and regeneration. Mitochondrial dysfunction in AT2 cells has been implicated in both chronic and acute injury-induced alveolar diseases, including idiopathic pulmonary fibrosis (IPF) and viral pneumonia. However, the role of mitochondrial homeostasis in post-injury lung repair and regeneration remains elusive. Here we demonstrate that genetic depletion of Ubiquitin Specific Peptidase 30 (USP30), a negative regulator of mitophagy, boosts mitophagy and restores mitochondrial function in AT2 cells, leading to protection from injury-induced apoptosis and enhanced stem cell activity. Both global and AT2-specific Usp30 knockout (KO) promote alveolar regeneration, protecting the mice from bleomycin-induced lung fibrosis and influenza pneumonia. Moreover, pharmacological inhibition of USP30 effectively alleviates these conditions. Together, our findings reveal a previously underappreciated role for mitophagy in lung injury and repair and highlight USP30 inhibition as a promising therapeutic strategy for treating alveolar diseases. - Source: PubMed
Publication date: 2026/04/14
Wu PeiChen JiaweiLiu LiWang PingLu TiantianShen ShengxiCao YiyuanSui YuandongLiu RunHuan XiajuanDing NingXi Ying - Lung microvascular endothelial inflammation and barrier dysfunction play critical roles in the pathogenesis of acute lung injury (ALI)/acute respiratory distress syndrome (ARDS). Despite recent scientific advances, the mortality of ALI/ARDS is still extremely high because the molecular mechanisms involved in ALI/ARDS remain unclear. In a recent issue of the journal Advanced Science, Baoyinna and colleagues reported that deubiquitinase USP30 induces lung microvascular inflammation and endothelial barrier disruption through the S-adenosylmethionine (SAM) cycle, DNA methylation, and miR-30a-5p down-regulation in ALI/ARDS. Their findings provide a strong rationale for targeting microRNAs, S-adenosylmethionine, DNA methylation, and deubiquitinating enzymes as potential therapeutic strategies for the treatment of ALI/ARDS. - Source: PubMed
Publication date: 2026/02/06
Su Yunchao - Intestinal ischemia-reperfusion (IIR) injury can cause intestinal barrier damage, systemic inflammatory response, and high mortality. The key mechanism is the disorder of the mitochondrial-endoplasmic reticulum network. Ubiquitin-specific peptidase 30 (USP30), located on the outer mitochondrial membrane, can reverse the partial ubiquitination of Parkin substrates or completely remove the ubiquitin chain to maintain mitochondrial function. Mitofusin 2 (MFN2) is a mitochondrial outer membrane fusion protein that mediates mitophagy and endoplasmic reticulum stress and participates in the formation of mitochondria-associated endoplasmic reticulum (MAMs). Our research showed that IIR reduces the protein expression of USP30 and MFN2, and overexpression of USP30 can increase the stability of MFN2 through deubiquitination and alleviate the damage caused by IIR. After overexpression of MFN2, mitochondrial dysfunction and endoplasmic reticulum stress caused by IIR are restored, while knockdown of MFN2 weakens the protective effect of USP30 on the MAMs. USP30 alleviates endoplasmic reticulum stress and mitochondrial dysfunction caused by intestinal ischemia-reperfusion injury by reducing the ubiquitination level of MFN2. The regulation of USP30 may be a promising strategy for alleviating intestinal ischemia-reperfusion injury. - Source: PubMed
Publication date: 2026/02/27
Weng ZiyiKadier TulanisaDing RuiliShi YuXie JingyuanChen RongMeng Qingtao - Polyamine homeostasis is tightly regulated by interconversion and catabolic pathways and has been increasingly implicated in neurodegenerative disorders, including Parkinson's disease (PD), where accumulation of α-synuclein (α-Syn) perturbs neuronal homeostasis. Spermidine/spermine N-acetyltransferase 1 (SAT1) occupies a central position in polyamine interconversion, and alterations in SAT1 activity have been linked to α-Syn toxicity and PD-related neuropathology. To investigate how SAT1 activity influences α-Syn-associated neurodegeneration, we employed a model of neuronal α-Syn expression. SAT1 overexpression reduced α-Syn protein levels, altered its subcellular distribution within the brain, and mitigated α-Syn-induced lifespan shortening. Transcriptomic analyses showed that SAT1 modulates stress-associated gene expression in the α-Syn background, including attenuation of chaperone and ubiquitin-related responses and coordinated changes in pathways linked to mitochondrial function and amino acid metabolism. SAT1 co-expression attenuated α-Syn-associated alterations in genes involved in mitochondrial quality control, including , , , and the mitochondrial ornithine carrier . At the protein level, SAT1 increased mitochondrial-associated signal, enhanced LC3 association with mitochondrial compartments, restored LC3-II/LC3-I ratios in mitochondrial fractions and reduced mitochondrial accumulation of α-Syn. Our findings indicate that SAT1 activity is associated with reduced α-Syn toxicity and altered mitochondrial-associated proteostasis during α-Syn expression. - Source: PubMed
Publication date: 2026/02/16
Bangash Zoya RMatsui HiroyoshiRanxhi BedriTodi Sokol VLeWitt Peter ATsou Wei-Ling - Interferon (IFN) signalling is essential for antiviral defence yet pathogenic in autoimmunity, however, the mechanisms orchestrating this duality remain poorly defined. Here, we identify , a cytoplasmic long non-coding RNA (lncRNA) induced by type I IFN, as a pivotal post-transcriptional amplifier of innate immunity. We demonstrate that selectively enhances the mRNA stability of nucleic acid sensors. Moreover, preferentially stabilizes the majority of AU-rich element (ARE)-containing interferon-stimulated gene (ISG) mRNAs. executes this function independently of its antisense partner, . The deletion of impaired IFN-β-mediated antiviral defence and suppressed pro-inflammatory cytokine production. Consistent with its role in amplifying immune responses, was markedly upregulated in human autoimmune diseases characterised by dysregulated IFN signalling, including systemic lupus erythematosus, rheumatoid arthritis, and dermatomyositis. Thus, our work unveils as a key regulator that fine-tunes the stability of nucleic acid sensors and ARE-containing immune transcripts, providing a direct mechanistic link between IFN signalling and post-transcriptional gene regulation. These findings establish as a critical rheostat for immune homeostasis and a promising therapeutic target for IFN-associated diseases. - Source: PubMed
Publication date: 2026/02/26
Pan JieFeng Min-YiXia TianJiang ShuaiZhu Peng-PengYu Xi-PingSu Zhi-HuiLiu YuWu Jia-QiZhao MingLi TaoXue WenYu YuChen LiangCai Hong