Ask about this productRelated genes to: PPAP2A antibody
- Gene:
- PLPP1 NIH gene
- Name:
- phospholipid phosphatase 1
- Previous symbol:
- PPAP2A
- Synonyms:
- PAP-2a, LPP1
- Chromosome:
- 5q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-02
- Date modifiied:
- 2016-10-05
Related products to: PPAP2A antibody
Related articles to: PPAP2A antibody
- Lipid phosphate phosphatases (LPPs) dephosphorylate lipid phosphates to regulate signaling and metabolism. Among the three mammalian isoforms, LPP1, LPP2, and LPP3, LPP2 has been strongly associated with cancer, making it a potential therapeutic target. However, the molecular mechanisms underlying its structural organization, substrate recognition, and catalysis remain elusive. Here, we report the cryo-EM structure of human LPP2 (hLPP2). hLPP2 assembles as a homo-tetramer, with phosphatidylcholine bound in the substrate pocket. The tetrameric arrangement provides a structural basis for LPP oligomerization. The wide, open-ended substrate pocket explains the enzyme's broad substrate specificity. Structural comparison with PAP2 family members, including hG6PC1 and ecPgpB, suggests a conserved catalytic mechanism and highlights the regulatory role of residue E159 in stabilizing the catalytic center and phosphate release. Collectively, these findings advance our understanding of the structural basis and enzymatic mechanism of LPPs and may provide insights for the development of novel cancer therapies. - Source: PubMed
Publication date: 2026/05/01
Wang WanyiXu YueGuo PeilinHan HanHan Lei - Lung cancer is the leading cause of cancer-related deaths worldwide, yet there has been little attention given to the correlation between the cancer transcriptome and the incidence and mortality of lung cancer across different geographic regions. - Source: PubMed
Zhang LingFan CongShang HuanxiaWang XiaojingZhang XinQiao QingzheNi JiajiaWu Shucai - Lipid phosphate phosphatases (LPPs) catalyze the dephosphorylation of a broad range of bioactive lipid phosphates, including lysophosphatidic acid and sphingosine-1-phosphate, playing essential roles in embryonic vasculogenesis, cell differentiation and inflammation. Here we present the cryo-electron microscopic structure of human LPP1 as a tetramer with C4 symmetry. We capture the phosphohistidine intermediate state by using vanadate as a phosphate analog, where vanadate is coordinated by positively charged residues from three conserved motifs (C1, C2 and C3). Structural investigations of LPP1 variants with mutations in two catalytic histidine residues confirm that the histidine in the C2 motif facilitates phosphate bond cleavage. Enzymatic assays validate our structural observations. Additionally, a phosphatidylinositol 4,5-bisphosphate (PIP) molecule was discovered in the LPP1 structure, underscoring a potential regulatory role for PIP in the catalytic activity of LPP1. - Source: PubMed
Publication date: 2026/01/09
Yang MengSun ChunpingHe YonglinQian Hongwu - Feline panleukopenia, caused by the highly lethal feline parvovirus (FPV), lacks effective prevention and treatment strategies. This study aimed to elucidate the key metabolic regulatory mechanisms during FPV infection. - Source: PubMed
Publication date: 2025/08/22
Sun ZhenZhu HongweiLiu YangZhang JianlongJiang LinlinYu XinYu JiayuZhang Xingxiao - Fat deposition is an important factor that affects meat production and quality in livestock and poultry. Long non-coding RNAs (lncRNAs) play an important role in duck fat deposition. The purpose of this study was to identify key lncRNAs and mRNAs involved in fat deposition of meat ducks based on whole transcriptome sequencing for intramuscular preadipocyte (IMP-0), intramuscular adipocyte after 4 days of induction (IMP-4), subcutaneous preadipocyte (SCP-0), and subcutaneous adipocyte after 4 days of induction (SCP-4). - Source: PubMed
Publication date: 2025/08/12
Zhou TingtingMeng XunhaoLiang WenshuangXue MinYang TianqiJiang YongBai HaoChang GuobinChen GuohongWang Zhixiu