Ask about this productRelated genes to: PEX19 Blocking Peptide
- 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 Blocking Peptide
Related articles to: PEX19 Blocking Peptide
- 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 - PEX19 is a cytosolic receptor that directs membrane proteins posttranslationally to peroxisomes, as well as to mitochondria, lipid droplets, and the endoplasmic reticulum. A comprehensive PEX19 interactome analysis uncovered PEX38 as an essential Euglenozoa-specific peroxin. PEX38 contains distinct domains that bind the cochaperone Hip and the PEX3-binding motif of PEX19, suggesting a role in stabilizing membrane proteins and preventing premature membrane docking. PEX38 illustrates functional repurposing in organelle biogenesis. It originated from a remnant of the GET/TRC pathway, typically responsible for the targeting of tail-anchored (TA) proteins to the endoplasmic reticulum. While most components of this machinery are absent in Euglenozoa, PEX38 has been retained and adapted to mediate peroxisomal membrane protein targeting. This evolutionary adaptation is unique to Euglenozoa. Because the PEX19-PEX38 interaction is essential for parasite viability and PEX38 has no human homologs, this complex is a promising therapeutic target against trypanosomatid parasites. - Source: PubMed
Publication date: 2026/02/26
Krishna Chethan KGaussmann StefanDas HirakJung MartinOeljeklaus SilkeSattler MichaelWarscheid BettinaKalel Vishal CErdmann Ralf - Peroxisomal or glycosomal membrane proteins (PMPs) depend on specific signal sequences, known as membrane peroxisomal targeting signals (mPTS), which are recognized by the cytosolic chaperone and import receptor PEX19. Computational prediction of PEX19-binding sites is a critical tool for identifying both known and novel PMPs and for advancing our understanding of the biogenesis of peroxisomes or glycosomes across diverse organisms, including humans, plants, fungi, and members of the Euglenozoa. PEX19-binding site prediction, including mPTS, is a computationally intensive process with broad applications, from identifying PMPs involved in essential cellular functions to uncovering pathogenic proteins in infectious agents, such as viruses, which interfere with the biogenesis or function of host cell peroxisomes. A web-based tool developed by Rottensteiner et al. previously enabled the prediction of PEX19-binding sites (PEX19BS), but it has become inaccessible, creating a significant gap for researchers aiming to identify and analyze these critical targeting motifs efficiently. To address this limitation, we have restored accessibility to a previously developed matrix-based prediction tool, now available as an open-access Google Colab notebook. This implementation enables efficient analysis and export of results, reinstating a valuable resource for studying membrane targeting in the biogenesis of peroxisomes and glycosomes. - Source: PubMed
Jeng SamanthaKrishna Chethan KErdmann RalfKalel Vishal C - Proximity labeling techniques, such as BioID and TurboID, have emerged as modern tools for studying protein-protein interactions (PPIs) in cells. TurboID is a highly efficient biotin ligase that biotinylates proximal proteins in living cells when fused to a bait protein. These biotinylated proteins are enriched using a pull-down assay with streptavidin beads and identified through proteomic analysis, revealing the interactome of the target protein. Here, we describe proximity labeling using TurboID fused to Trypanosoma brucei PEX19, an essential cytosolic protein and a receptor for newly synthesized glycosomal membrane proteins, to identify its interactome. Understanding these interactions can be crucial for identifying new drug targets to combat these parasites. This powerful approach for mapping interactomes can be applied broadly to other organisms, including plants, yeast, and mammalian systems. - Source: PubMed
Krishna Chethan KErdmann RalfKalel Vishal C - Perfluorooctanesulfonic acid (PFOS) is an environmental pollutant of significant concern in the field of reproductive health. Our previous studies have confirmed that PFOS can induce mitochondria-dependent ferroptosis, thereby impairing oocyte maturation and embryonic development. This study investigated the protective effects of exogenous glycine (Gly) supplementation-an important endogenous antioxidant-on PFOS-induced damage in porcine oocytes. Initially, we found that Gly alleviated the adverse effects of PFOS exposure on oocyte maturation quality and blastocyst development. Further studies demonstrated that exogenous Gly supplementation significantly improved mitochondrial function, increased adenosine triphosphate (ATP) and glutathione (GSH) levels, and markedly reduced reactive oxygen species (ROS) levels, indicating that Gly attenuates PFOS-induced mitochondrial oxidative damage in oocytes. Moreover, PFOS exposure significantly decreased ferritin levels, dysregulated iron (Fe²⁺) homeostasis, and triggered ferroptosis-all of which were ameliorated by exogenous Gly supplementation. Gly also mitigated PFOS-induced abnormalities in the expression of ferroptosis-related genes such as PCBP1, PCBP2, GCLC, and SLC7A11. In addition, the aberrant expression of Nrf2, PEX19, GPX4, and malondialdehyde (MDA) caused by PFOS exposure was reversed after Gly supplementation. In conclusion, glycine enhances antioxidant capacity by regulating redox balance, inhibits lipid peroxidation, improves ferroptosis-related conditions, and thereby mitigates the detrimental effects of PFOS exposure on in vitro oocyte maturation and early embryonic development. - Source: PubMed
Publication date: 2025/11/04
Sun XiaoqingTeng RanXu NingZhang EnboChen XingfuLi Suo