Ask about this productRelated genes to: PEX3 Blocking Peptide
- Gene:
- PEX3 NIH gene
- Name:
- peroxisomal biogenesis factor 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 6q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-21
- Date modifiied:
- 2014-11-19
Related products to: PEX3 Blocking Peptide
Related articles to: PEX3 Blocking Peptide
- Mitochondrial-derived vesicles (MDVs) mediate selective trafficking of mitochondrial proteins and lipids to other organelles and contribute to organelle communication and mitochondrial quality control. While MDVs that deliver mitochondrial cargo to lysosomes have been extensively studied, the diversity of MDV pathways linking mitochondria to peroxisomes remains poorly understood. In particular, it is unclear how MDV pathways targeting peroxisomes relate to those delivering cargo to lysosomes, and whether cargos targeted to pre-existing peroxisomes utilize the same vesicular intermediates that participate in de novo peroxisome biogenesis. Here we examined MAPL trafficking using a peroxisome reconstitution system in PEX3-deficient fibroblasts. We found that MAPL is excluded from PEX3-positive pre-peroxisomal vesicles and instead is delivered to pre-existing peroxisomes, indicating that MAPL trafficking occurs through a pathway distinct from vesicles that initiate peroxisome formation. Structure-function analysis further revealed that a C-terminal amphipathic helix within MAPL is required for efficient targeting to peroxisomes. SNX9 depletion impaired both MAPL delivery to pre-existing peroxisomes and stress-induced lysosomal MDV pathways, whereas VPS35 depletion selectively reduced MAPL delivery without affecting lysosomal MDV pathways. In contrast, Parkin depletion impaired lysosomal MDV pathways but did not influence MAPL trafficking. Together, these findings demonstrate that mitochondria generate multiple classes of MDVs that are sorted into mechanistically distinct trafficking routes linking mitochondria with peroxisomes and lysosomes. - Source: PubMed
Publication date: 2026/05/12
Sugiura AyumuNakamura KohtaMcBride Heidi MOkazaki Yasushi - 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 - Peroxisomes are eukaryotic organelles primarily known for their conserved roles in fatty acid β-oxidation and hydrogen peroxide detoxification. These organelles are also involved in a diverse range of other metabolic and non-metabolic functions. We recently compared the transcriptome and proteome of Saccharomyces cerevisiae wild-type and peroxisome-deficient (pex3) cells. This study uncovered the major processes and metabolic pathways that are influenced by peroxisomes. Here we performed a mass spectrometry-based analysis of intracellular metabolites of the same two strains. This led to the identification of 160 compounds, of which seven exhibited significant differences between wild-type and pex3 cells (glycerol-3-phosphate, carnitine, pantothenate, acetyl-spermidine, propionyl-carnitine, and aminolevulinic acid). Notably, we observed elevated lysine levels in pex3 cells, consistent with previous findings, which confirms the reliability and accuracy of our analytical approach. In addition, changes in carnitine compounds were measured, aligning with the proposed occurrence of a carnitine shuttle across the peroxisomal membrane. By integration of the current metabolomic data with the previously obtained transcriptomic and proteomic data, we provide a broader view of the metabolic impact of peroxisome deficiency. We show that, in addition to the well-known function of yeast peroxisomes in lipid and fatty acid degradation, these organelles are also involved in lipid synthesis. Furthermore, our study revealed that peroxisome deficiency affects polyamine homeostasis. - Source: PubMed
Publication date: 2026/01/29
Kosir TjasaMalheiro Daniel Baptista AlvesJohnsen Lea GiørtzDas HirakWarscheid BettinaDanielsen Mortenvan der Klei Ida J - Androgenetic alopecia (AGA) represents the most prevalent multifactorial condition leading to hair loss, necessitating an enhanced molecular understanding. The aim of this study is to present the analysis integrating protein, mRNA and miRNA between frontal and occipital regions of patients with androgenetic alopecia (AGA) and to identify potential mechanism. Paired frontal and occipital scalps from four male donors with AGA were collected for transcriptomic and proteomics analyses. The molecular and protein characteristics of AGA were demonstrated by a comprehensive bioinformatics approach. Additionally, immunofluorescence (IF) and dual-luciferase reporter (DLR) assays were employed to confirm the analytical findings. A total of 758 differentially expressed proteins (DEPs), 1802 differentially expressed mRNAs (DERs) and 61 differentially expressed miRNAs (DEmiRNAs) were identified. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses revealed significant enrichments in lipid metabolism, especially those involving PPAR signaling. Co-expression analyses further supported the association of up-regulated genes with lipid metabolism. A protein-protein interaction network analysis, supplemented by KEGG enrichment and the MCE algorithm, pinpointed four candidate genes: , , and . IF confirmed significant upregulation of ACAA1 and PEX3 in scalp tissues with AGA, while IDH1 was downregulated and DBI without significant changes. A competing endogenous RNA network indicated that hsa-miR-1343-3p targets and hsa-miR-3609_R-2 targets , which were confirmed by DLR assays. This study provides preliminary evidence that hsa-miR-1343-3p-mediated regulation of contributes to AGA pathogenesis, suggesting a link between AGA and lipid metabolism. - Source: PubMed
Publication date: 2026/01/12
Yang Xiao-ShuangDuan LiyangMiao Yu-JieLu ZhongfaDai Ru - Loss-of-function mutations in have been associated with Zellweger syndrome (ZS), a severe form of peroxisome biogenesis disorder (PBD) characterized by significant global developmental delay, muscle weakness with bilateral ptosis, cholestasis, hypotonia, and seizures. ZS can be life-threatening if manifested in the neonatal period. - Source: PubMed
Publication date: 2026/01/06
Su JinfengTao YingboZhang LianLuo Jun