Ask about this productRelated genes to: PEX19 antibody
- Gene:
- PEX19 NIH gene
- Name:
- peroxisomal biogenesis factor 19
- Previous symbol:
- PXF
- Synonyms:
- HK33, D1S2223E, PMP1, PMPI, PXMP1
- Chromosome:
- 1q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-06-12
- Date modifiied:
- 2016-10-05
Related products to: PEX19 antibody
Related articles to: PEX19 antibody
- The effect of thyroid hormones (TH) on metabolism and energy balance relies on their impact on lipid storage in adipose tissue (AT). Since peroxisomes play a key role in lipid metabolism in white AT, hypothyroidism may critically influence peroxisome population/dynamics. This study aimed to determine depot- and time-dependent effects of methimazole-induced hypothyroidism on peroxisome biogenesis and remodeling in rat white AT. Hypothyroidism was induced using 0.04% methimazole over 7, 15, or 21 days. We show that hypothyroidism affects peroxisome biogenesis in subcutaneous AT (SAT) and visceral AT (VAT) (mesenteric-mVAT, retroperitoneal-rVAT and gonadal-gVAT) in a depot-specific manner. Firstly, although a gradual increase in peroxisomal number is present in all of the AT depots examined, the time course differs. Secondly, according to ultrastructural and protein expression analyses of Pex11β, Pex19, and PPARα, biogenesis pathways are switching from canonical to de novo pathway in hypothyroidism, again distinctively across particular depots. Furthermore, this is accompanied by the emergence of unusual peroxisomal structures (pexopodium) infiltrating lipid bodies in VAT. The absence of acyl-coenzyme A oxidase 1 (ACOX1) suggests that such structures may develop as a consequence of uncoordinated oxidation of accumulated fatty acids in VAT. The presence of pexopodium was increased from day 15 of hypothyroidism in mVAT. However, this increase was transient in rVAT and gVAT, indicating different peroxisomal dynamics between VAT depots during the monitored period of induction. Pexopodium-like structures were not observed in SAT. Our results identify peroxisomal remodeling as a previously underappreciated component of adipose tissue plasticity in hypothyroidism. Discrete temporal and depot-specific responses, including the formation of pexopodia in VAT, underscore the functional heterogeneity of white AT depots and suggest that peroxisomal dynamics may contribute to regional metabolic vulnerability under thyroid hormone deficiency over the time. - Source: PubMed
Publication date: 2026/07/23
Addloli AhseinIlic MarijaZakic TamaraKorac BatoCvoro AleksandraJankovic AleksandraKorac Aleksandra - The kidney is an organ rich in peroxisomes, which play a pivotal role in fatty acid oxidation and ROS decomposition. Importantly, peroxisomal dysfunction contributes to the development and progression of various renal diseases. Therefore, we aimed to elucidate whether peroxisomes affect renal damage and fibrosis over time using a unilateral ureteral obstruction (UUO) mouse model. - Source: PubMed
Publication date: 2026/06/25
Kim JinhwiKim HyunsooChhetri ArunManandhar LaxmanJang GyuhoPark ChannyPark Raekil - Barth Syndrome (BTHS) is an inherited mitochondrial cardiomyopathy caused by variants in the gene encoding TAFAZZIN (Taz), a transacylase catalyzing the synthesis of the essential mitochondrial phospholipid cardiolipin (CL). Although defects in Taz deteriorate mitochondrial respiration, Ca-uptake, and redox regulation in cardiac myocytes, we previously observed an unexpected lack of oxidative cardiac damage, despite the development of cardiomyopathy in a BTHS mouse model with Taz-knockdown (KD). Furthermore, we revealed that the integrated stress response (ISR) governs metabolic rewiring in Taz-KD hearts to compensate for deficient mitochondrial FAO and to support GSH production. Here, we interrogated whether adaptive mechanisms in peroxisomes, which are closely associated with mitochondria and harbor antioxidative enzymes, can also compensate for the mitochondrial defects. We identified alterations in the peroxisomal biogenesis factors PEX14 and PEX19, indicating changes in the peroxisomal proteome in Taz-KD vs. WT hearts. While the enzymes of peroxisomal FAO were unchanged, levels of Lon Protease 2 (LONP2) and catalase were elevated in Taz-KD hearts. Inhibition or siRNA-mediated knockdown of catalase increased reactive oxygen species (ROS) and blunted the protection of mouse embryonic fibroblasts (MEF) with Taz-knockout (KO), but not in WT, from ROS-induced activation of the apoptotic caspase 3. Furthermore, we observed that the increase in plasmalogen synthesis in cardiac Taz-KD peroxisomes contributes to the activation of the ISR, since siRNA-mediated knockdown of the key enzyme GNPAT blunted the ISR and thereby increased cellular ROS in Taz-KO, but not WT MEFs. In conclusion, peroxisomes facilitate a counterregulatory response to dysfunctional mitochondria by activating a catalase-driven ROS defense and maintaining ISR-mediated metabolic alterations, both of which compensate for mitochondrial dysfunction and oxidative stress. Therefore, the so far poorly investigated mitochondrial-peroxisome crosstalk may represent a novel therapeutic target in an orphan disease with a poor prognosis. - Source: PubMed
Publication date: 2026/06/30
Kajese ElsieHachmann MalteErmer Katharina JErk ManuelaAlhasaan LinKohlhaas MichaelBömmel HeikeBerberich LisaCarlein ChristopherEberl HannaStreckfuß-Bömeke KatrinRoma Leticia PratesErgün SüleymanMaack ChristophKarnati SrikanthDudek Jan - Yeast cells rely on the actomyosin machinery to mediate organelle motility. The type V myosin motor Myo2p transports organelles along actin cables from the mother cell to the nascent bud. To facilitate this process, organelles have evolved specific adaptor proteins that link them to the cargo-binding domain of Myo2p. Peroxisomes use two such adaptors: Inp2p, the principal determinant of peroxisome inheritance, and the biogenesis factor Pex19p, which has been assigned a secondary role in peroxisome partitioning. Here, we identify a regulatory function for the peroxisome biogenesis factor Pex3p in controlling peroxisome inheritance in the budding yeast, . Pex3p is an integral membrane protein that contains a cytosol-exposed surface loop subject to phosphorylation. This loop is essential for the recruitment of both Inp2p and Pex19p. Phosphorylation of serine residues within the loop in response to environmental stimuli abolishes Inp2p binding to, and markedly reduces Pex19p association with, Pex3p, thereby reducing the efficiency of peroxisome partitioning between the mother cell and the bud. Deleting the loop in Pex3p completely abolishes peroxisome segregation. By serving as a membrane anchor for the recruitment of both inheritance factors Inp2p and Pex19p, Pex3p exerts a critical level of control over peroxisome partitioning. - Source: PubMed
Publication date: 2026/05/28
Knoblach BarbaraRachubinski Richard A - Peroxisomes are vital cellular organelles that play critical roles in metabolism, immune regulation, and disease pathogenesis. As a key receptor for peroxisomal membrane proteins, peroxisomal biogenesis factor 19 (PEX19) is essential for peroxisome biogenesis. In this study, we identify PEX19 as a novel host restriction factor against porcine deltacoronavirus (PDCoV), an emerging enteropathogenic coronavirus with zoonotic potential. Overexpression of PEX19 significantly inhibits PDCoV replication, while knockout of PEX19 enhances viral propagation. Interestingly, the anti-PDCoV effect of PEX19 largely depends on its farnesylation modification, as PEX19 mutants with deleted or mutated farnesylation sites exhibit only marginal anti-PDCoV activity. Mechanistically, PEX19 restricts PDCoV infection through three distinct pathways: (i) reducing cellular cholesterol levels in a farnesylation-dependent manner, (ii) targeting the viral nonstructural protein 2 (nsp2) for autophagy-lysosome-mediated degradation, which is also dependent on farnesylation, and (iii) inducing low-level interferon production independently of farnesylation. Taken together, these findings define a new antiviral role for PEX19 and highlight its potential as a therapeutic target for combating PDCoV infection.IMPORTANCEPeroxisomes are increasingly recognized as critical regulators of virus-host interactions; however, their roles during coronavirus infection remain poorly understood and controversial. By screening the peroxins (PEXs) that regulate the replication of porcine deltacoronavirus (PDCoV), we identify PEX19, a key peroxisomal biogenesis factor, as a novel antiviral host protein, whose anti-PDCoV activity is largely dependent on farnesylation modification. Our findings demonstrate that farnesylated PEX19 restricts PDCoV replication by reducing cellular cholesterol levels and promoting autophagy-lysosome-mediated degradation of the viral nsp2 protein, while also inducing low-level interferon production independently of farnesylation. These results provide new molecular insights into PDCoV-host interactions and highlight PEX19 as a potential therapeutic target against PDCoV infection. - Source: PubMed
Publication date: 2026/03/24
Chen ChaoqunSu GuanningWang YuchenXiong YuanxiangXiao WenwenLi ZhuangFang LiurongZhou YanrongXiao Shaobo