Ask about this productRelated genes to: VAC14 antibody
- Gene:
- VAC14 NIH gene
- Name:
- VAC14 component of PIKFYVE complex
- Previous symbol:
- TAX1BP2
- Synonyms:
- FLJ10305, ArPIKfyve
- Chromosome:
- 16q22.1-q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-09
- Date modifiied:
- 2019-04-15
Related products to: VAC14 antibody
Related articles to: VAC14 antibody
- Cervical cancer (CESC) is a major gynecological malignancy, and abnormalities in phosphoinositide metabolism (PPM) are closely linked to tumor progression. This study aimed to screen phosphoinositide metabolism-related genes (PPM-RGs) with prognostic value for CESC and explore their molecular mechanisms and clinical significance. - Source: PubMed
Publication date: 2026/07/09
Meng HuiTan LiChen YingWang DongmeiQi YongZhu Chuchao - Osteosarcoma is the malignant bone neoplasm affecting pediatric and adolescent with unsatisfactory five-year survival. Dysregulated phospholipid metabolism is crucial for membrane integrity, signaling, and energy homeostasis, contributinga range of cancers' progression. Nevertheless, itsrolein osteosarcoma persists uncertain. The investigation aims to identify phospholipid metabolism-related signature genes for osteosarcoma and evaluate their prognostic value and therapeutic potential. - Source: PubMed
Publication date: 2026/06/24
Liang YihuiBa YiwenZhou QiweiXuan JiangweiNi WenfeiWu ChenyuZhan Jingdi - Ethanol stress in Saccharomyces cerevisiae induces a rapid morphological transition in the vacuole from a multilobed (2-3 lobes) structure to a unilobed form. This change reflects a shift in the dynamic equilibrium between vacuolar fusion and fission, towards fusion. The process is mediated by inhibition of the fission machinery, as cells pre-conditioned with ethanol retain enlarged vacuoles even upon subsequent exposure to vacuole fission-inducing agents, indicating a block in vacuole fragmentation. This inhibition is progressive, as prolonged ethanol exposure results in an increasingly pronounced fission block. The underlying mechanism involves the downregulation of Fab1, a lipid kinase responsible for synthesizing phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P₂), a key phospholipid regulator facilitating vacuole fission. Ethanol-induced modulation of PtdIns(3,5)P₂ pools is indicated by the redistribution of this lipid's sensor away from the vacuole membrane. This redistribution is prevented in the presence of the hyperactive mutant Fab1*, which produces elevated PtdIns(3,5)P₂. The concomitant delayed vacuole enlargement under ethanol stress in cells expressing Fab1* supports ethanol-induced suppression of PtdIns(3,5)P₂ levels. Reduced levels of PtdIns(3,5)P₂ promote dissociation of this lipid's effector, Atg18, from the vacuole membrane. There is also uncoupling of Atg18 from the Fab1 complex via disrupted interaction with the Vac14 scaffold. Further, ethanol exposure induces differential phosphorylation of Atg18, thereby altering its affinity for PtdIns(3,5)P₂. Consequently, ethanol rapidly remodels vacuole morphology by simultaneously reducing PtdIns(3,5)P₂ abundance and weakening effector-lipid interactions. This concerted mechanism ensures a rapid inhibition of vacuole fission in the presence of ethanol. - Source: PubMed
Publication date: 2026/06/11
Mandal PrithaHazra BabaiSett AnurupaPatra NabanitaGhosh TrishaSil Alok KumarSarkar Srimonti - Phosphatidylinositol 3,5-bisphosphate [PI(3,5)P] is a lysosomal signaling lipid whose deficiency, caused by mutations in the PIKfyve complex subunits FIG4 or VAC14, underlies a spectrum of fatal neurologic diseases including Charcot-Marie-Tooth type 4J (CMT4J) and amyotrophic lateral sclerosis (ALS). To map the molecular consequences of PI(3,5)P insufficiency in the brain, we performed quantitative proteomic and transcriptomic analyses of three mouse lines bearing distinct loss-of-function mutations in Fig4 or Vac14, examining the brain at the presymptomatic and end stages. Strikingly, profound neuroinflammation was already present at postnatal day 5 (before significant neurodegeneration), characterized by complement activation, interferon signaling, and parenchymal infiltration of peripheral myeloid cells and T-cells. Isolated mutant microglia exhibited a markedly pro-oxidative transcriptional state with elevated reactive oxygen species, a partly non-cell-autonomous phenotype, being present in microglia from mice with conditional Fig4 inactivation in just neurons and astrocytes. Comparison of early (P5) and late (P25) proteomics data revealed that PI(3,5)P insufficiency impairs developmental remodeling of the brain proteome: proteins typically upregulated during postnatal maturation failed to accumulate, implicating lysosomal function in neurodevelopment. We identify coordinated elevation of p53, Fas receptor, inflammatory caspases, Gasdermin D, RIPK1, and ZBP1, consistent with multifactorial inflammatory cell death with features of apoptosis, pyroptosis, and necroptosis. Many of the dysregulated proteins are encoded by genes mutated in lysosomal storage disorders, ALS, CMT, Alzheimer's and Parkinson diseases, extending the pathogenic relevance of PI(3,5)P insufficiency. Together, these findings establish that early neuroinflammation is a defining - and likely initiating - feature of neurodegeneration caused by disruption of lysosomal PI(3,5)P. - Source: PubMed
Publication date: 2026/06/03
Wong BridgetPayne MorganSilva AlexanderKurniawan EmmaEidman Alison SPizzo DonaldRajupalem RachanaLenk Guy MPaulo Joao AKhan TaimurEskelinen Eeva-LiisaGygi Steve PBrown Nicholas GMeisler Miriam HMendiola Andrew SGassaway Brandon MFerguson Cole J - The high prevalence of cancer immunotherapy resistance, coupled with substantial tumor heterogeneity, underscores the urgent need for innovative therapeutic targets. A deeper understanding of immunoregulatory mechanisms would provide new targets and combination therapeutic strategies for tumor therapy. In this study, we demonstrate that HSD17B12 enhances anti-tumor immunity and represents a promising therapeutic target. Mechanistically, HSD17B12 promotes lysosome-dependent degradation of PD-L1 via the VAC14 and ESCRT complexes across various malignancies, regardless of its 3-ketoacyl-CoA reductase activity. HSD17B12-deficient cells displayed PD-L1 accumulation in both tumor cells and exosomes, reducing T cell-mediated cytotoxicity. Notably, we found a significant negative correlation between HSD17B12 and PD-L1 expression in colorectal cancer tissues. Furthermore, high HSD17B12 expression in CRC correlated with increased infiltration of cytotoxic T cells. Based on these findings, we designed a peptide, HSD-CC1-NPGY, which effectively reduces PD-L1 expression in cells and suppresses tumor growth in a mouse model. Overall, our results establish HSD17B12 as an important regulator of anti-tumor immunity and a promising therapeutic target for cancer treatment. - Source: PubMed
Publication date: 2026/01/27
Zhou ZhihuiLu YingLi PanLiu XinCheng WeiChen Hai-NingDai LunzhiRen Haiyan