Ask about this productRelated genes to: TUSC4 antibody
- Gene:
- NPRL2 NIH gene
- Name:
- NPR2 like, GATOR1 complex subunit
- Previous symbol:
- TUSC4
- Synonyms:
- NPR2L, NPR2
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-20
- Date modifiied:
- 2017-06-13
Related products to: TUSC4 antibody
Related articles to: TUSC4 antibody
- This study aimed to investigate the mechanisms by which Citrus aurantium honey modulates gastrointestinal motility, inflammation, and barrier function using network pharmacology and Drosophila melanogaster models. - Source: PubMed
Publication date: 2026/06/01
Wan WenqiHuang RuiguangCao ShuqiongPan LuxiaZhang WenkaiJiang WujunLiu Zhiyong - To determine the diagnostic yield of genetic testing in patients undergoing presurgical evaluation for epilepsy. - Source: PubMed
Publication date: 2026/05/20
Jünemann ClaraStuart AmandaKaur NavprabhjotWiebe SamuelJette NathalieSingh ShailyBorlot FelippeKnake Susanne Billie Au Ping YeeKlein Karl Martin - The mTOR pathway is important for neurodevelopment. The GATOR1 complex, composed of DEPDC5, NPRL2, and NPRL3, functions as a negative regulator of mTORC1 activity and pathogenic variants in the genes which comprise this complex cause focal epilepsy and malformation of cortical development, all named as GATORopathies. While focal cortical dysplasia is commonly reported, the full spectrum of associated neuroimaging findings remains incompletely defined. - Source: PubMed
Publication date: 2026/05/18
Rb RevanthAjith AdityaNayak AbhishekRadhakrishnan AshalathaThomas BejoyKesavadas Chandrasekharan - Acute activation of mTORC1 by amino acids (AAs) is pivotal for growth regulation, yet it remains unclear how the intracellular nutrient-sensing machinery might be rewired by environmental cues to execute distinct functions. Here we report that, despite nutrient insufficiency, cancer-intrinsic AA-sensing mTORC1 signalling is hijacked by inflammatory cytokines in the tumour microenvironment (TME). ZBTB5 translates inflammatory signals to restore mTORC1 pathway via disrupting the GATOR1 complex. Mechanistically, inflammatory cues promote phosphorylation of ZBTB5-S127, thereby recruiting the Cullin3 E3 ubiquitin ligase to degrade NPRL2 within GATOR1 and reactivate mTORC1 signalling. Consequently, tumoural AA uptake is boosted to exacerbate nutrient restriction and death of CD8 T cells, leading to immunoevasion, tumour progression and inferior response to immune-checkpoint inhibitors. As such, blocking ZBTB5-pS127 ameliorates primary and acquired resistance to checkpoint blockade. Thus, targeting aberrant nutrient-sensing via the ZBTB5-pS127-mTORC1 axis represents a proof-of-concept strategy to sensitize cancer immunotherapy by alleviating AA restriction in the TME. - Source: PubMed
Publication date: 2026/04/03
Xiang JunyuWang TaoTian ShuoranLi JinyangLuo MengyunWang YuzhuDu AibeiChen XuTian FanxuanWang LeiZhang YongchaoHan MengyiHou WenqingWang XinyuHou TaoLiu QinChen DongfengWen LiangzhiQin ZhongyiLi XianfengJiang CongZhang QiaoqiaoLiu PengdaBian XiuwuWei WenyiWang Bin - Host factors that directly target viral immune antagonists are crucial for antiviral defense. In this study, we identify NPRL2 as a novel host restriction factor that directly interacts with the porcine reproductive and respiratory syndrome virus (PRRSV) protein Nsp1α, a key viral virulence factor. This interaction is mediated by the C-terminal domain of NPRL2 and the PCPα domain of Nsp1α. Functional studies demonstrated that NPRL2 overexpression inhibits PRRSV replication, while its knockdown enhanced viral propagation. Mechanistically, NPRL2 acts as a bridge, mediating K63-linked ubiquitination of Nsp1α at lysine 150 and subsequently recruiting the autophagic machinery for its degradation. This process was confirmed by monitoring LC3-II conversion and autophagic flux. Our findings reveal a precise mechanism by which NPRL2 antagonizes PRRSV by targeting a critical viral protein for autophagic degradation, highlighting the therapeutic potential of harnessing the host's ubiquitin-autophagy pathway to combat viral infections. - Source: PubMed
Publication date: 2026/02/25
Yi HeyouWang ShaojunWang QiumeiLu LechenXie ErminYe RuiruiWang HengZhang Guihong