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Updated: Aug 30, 2026

Monitoring Stub1-Mediated Pexophagy
Published on: May 12, 2023
Novel mutations in the PEX12 gene of patients with a peroxisome biogenesis disorder
Jeannette Gootjes1, Frank Schmohl, Hans R Waterham
1Department of Clinical Chemistry, Academic Medical Center, University of Amsterdam, The Netherlands.
Insights
Peroxisome biogenesis disorders (PBDs) linked to PEX12 gene mutations show varied severity. Novel PEX12 mutations correlate with specific PBD phenotypes and biochemical markers in patients.
Area of Science:
- Genetics
- Molecular Biology
- Biochemistry
Background:
- Peroxisome biogenesis disorders (PBDs) are a group of genetic diseases with diverse clinical presentations.
- Zellweger syndrome (ZS), neonatal adrenoleukodystrophy (NALD), and infantile Refsum disease (IRD) are key PBD variants.
- Defects in at least 11 genes cause PBDs, impacting peroxisome function.
Purpose of the Study:
- To investigate the genetic basis of PBDs in complementation group 3 (CG3) patients.
- To identify novel mutations in the PEX12 gene and correlate them with clinical and biochemical phenotypes.
- To understand the functional impact of PEX12 mutations on peroxisomal protein import.
Main Methods:
- Genetic analysis of the PEX12 gene in five CG3 patients.
- Sequence analysis to identify mutations in PEX12.
- Biochemical assays in patient fibroblasts to measure DHAPAT activity and beta-oxidation of very long-chain fatty acids and pristanic acid.
Main Results:
- Five distinct PEX12 mutations were identified in five CG3 patients, with four being novel.
- Mutations leading to truncated PEX12 protein lacking the zinc-binding domain were associated with severe phenotypes (ZS/NALD).
- A patient with a milder phenotype (IRD) possessed PEX12 alleles encoding a functional zinc-binding domain.
- Genotypes correlated well with biochemical markers (DHAPAT activity, C26:0 and pristanic acid beta-oxidation) and clinical outcomes.
Conclusions:
- PEX12 mutations are a significant cause of PBDs in CG3.
- The location and nature of PEX12 mutations, particularly the presence of the zinc-binding domain, determine disease severity.
- Genotype-phenotype correlations in PEX12-related PBDs are strong, aiding in diagnosis and prognosis.
Abstract:
The peroxisome biogenesis disorders (PBDs) form a genetically and clinically heterogeneous group of disorders due to defects in at least 11 distinct genes. The prototype of this group of disorders is Zellweger syndrome (ZS), with neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD) as milder variants. Liver disease, variable neurodevelopmental delay, retinopathy and perceptive deafness are common to PBDs. PBD patients belonging to complementation group 3 (CG3) have mutations in the PEX12 gene, which codes for a protein (PEX12) that contains two transmembrane domains, and a zinc-binding domain considered to be important for its interaction with other proteins of the peroxisomal protein import machinery. We report on the identification of five PBD patients belonging to CG3. Sequence analysis of their PEX12 genes revealed five different mutations, four of which have not been reported before. Four of the patients have mutations that disrupt the translation frame and/or create an early termination codon in the PEX12 open reading frame predicted to result in truncated protein products, lacking at least the COOH-terminal zinc-binding domain. All these patients display the more severe phenotypes (ZS or NALD). The fifth patient expresses two PEX12 alleles capable of encoding a protein that does contain the zinc-binding domain and displayed a milder phenotype (IRD). The three biochemical markers measured in fibroblasts (DHAPAT activity, C26:0 beta-oxidation and pristanic acid beta-oxidation) also correlated with the genotypes. Thus, the genotypes of our CG3 patients show a good correlation with the biochemical and clinical phenotype of the patients.
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