Ask about this productRelated genes to: PEX7 antibody
- Gene:
- PEX7 NIH gene
- Name:
- peroxisomal biogenesis factor 7
- Previous symbol:
- -
- Synonyms:
- PTS2R, RD
- Chromosome:
- 6q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-05-22
- Date modifiied:
- 2016-10-05
Related products to: PEX7 antibody
Related articles to: PEX7 antibody
- Peroxisomes are single-membrane organelles present in most eukaryotic cells and play important roles in various biological activities. PEX5 and PEX7 are peroxisomal receptors that import matrix proteins containing peroxisomal targeting signals into the peroxisome. However, the specific contributions of CgPEX5 and CgPEX7 in the growth, nutritional utilization, conidial development, and pathogenicity of Colletotrichum gloeosporioides remain to be elucidated. Our results demonstrated that deletion of Cgpex5 or Cgpex7 severely inhibited vegetative growth of C. gloeosporioides. However, compared to the ΔCgpex7 strain, the ΔCgpex5 exhibited reduced capacity for carbon and nitrogen sources utilization, lower conidial production, aberrant conidial morphology and downregulated expression of CgBrlA, CgAbaA and CgWetA in C. gloeosporioides. Transcriptome analysis further indicated that Cgpex5 deletion triggered a reprogramming of crucial metabolic pathways, resulting in altered expression of multiple key metabolism-related genes. In addition, the ΔCgpex5 strain exhibited reduced penetration ability, induced smaller lesions on the host, and led to lower levels of host-derived reactive oxygen species (ROS) during infection compared to the ΔCgpex7 strain. Taken together, our results demonstrate that Cgpex5 gene is essential for growth, nutritional utilization, conidial development, and pathogenesis in C. gloeosporioides, whereas Cgpex7 plays a comparatively minor role. These findings indicated that Cgpex5-mediated peroxisomal import pathway represents a promising target for developing novel fungicidal strategies to control postharvest diseases. - Source: PubMed
Publication date: 2026/03/14
Han ZhanhongRen DandanZhu PinkuanGong DiZhang ZhengkePan Yonggui - Rhizomelic chondrodysplasia punctata type 1 (RCDP1) is a peroxisomal disorder characterized by skeletal shortening, intellectual disability, seizures, cataracts, and reduced lifespans. RCDP1 is caused by biallelic loss-of-function variants in , which encodes a protein required for importing select enzymes into the peroxisome matrix, including those essential for ether lipid synthesis (e.g., plasmalogens) and the branched-chain fatty acid catabolism. Plasmalogen deficiency is a hallmark of RCDP1 and other peroxisomal disorders, including RCDP types 2-5 (RCDP2-5) and Zellweger spectrum disorders (ZSD). Here, we performed comprehensive metabolomic profiling of clinical samples from RCDP patients and -deficient mouse models. We identified profound neurometabolic disturbances in the cerebral cortex and cerebellum of -deficient mice involving multiple lipid classes, including phosphatidylethanolamines (PEs), phosphatidylcholines (PCs), acylcarnitines, and sphingomyelins. Notably, many of these neurometabolic alterations were absent in patient and -deficient mouse plasma, indicating that plasma-based profiling can underrepresent the extent of CNS lipid remodeling. Overall, these findings reveal novel insights into neurometabolic adaptations to plasmalogen deficiency and suggest the potential involvement of additional pathways that may contribute to neurological dysfunction in RCDP. - Source: PubMed
Publication date: 2025/12/19
Sankhe RiyaWilliams Meredith IFallatah WedadMackay LauraBrown Mary LayneBhagwat PranjaliElsea Sarah HBraverman NancyWangler Michael F
- Source: PubMed
- Peroxisomes are metabolic organelles essential for human health. Defects in peroxisomal biogenesis proteins (also known as peroxins (PEXs)) cause devastating disease. PEX7 binds proteins containing a type 2 peroxisomal targeting signal (PTS2) to enable their import from the cytosol into peroxisomes, although many aspects of this process remain enigmatic. Utilizing in vitro assays, yeast and human cells, we show that PEX39, a previously uncharacterized protein, is a cytosolic peroxin that facilitates the import of PTS2-containing proteins by binding PEX7 and stabilizing its interaction with cargo proteins containing a PTS2. PEX39 and PEX13, a peroxisomal membrane translocon protein, both possess an (R/K)PWE motif necessary for PEX7 binding. Handover of PEX7 from PEX39 to PEX13 via these motifs provides a new paradigm for peroxisomal protein import and biogenesis. Collectively, this work reveals how PEX39 and (R/K)PWE motifs facilitate the import of PTS2-containing proteins and advances our understanding of peroxisomal disease. - Source: PubMed
Publication date: 2025/07/30
Chen Walter WRodrigues Tony AWendscheck DanielPedrosa Ana GYang ChendongFrancisco TâniaMöcklinghoff TillZografakis AlexandrosNunes-Silva BernardoAvraham Reut ESilva Ana RFerreira Maria JDas HirakKoster JanetNeuwirth SimoneBender JulianOeljeklaus SilkeSondhi VarunGatsogiannis ChristosSchuldiner MayaZalckvar EinatHofmann KayWaterham Hans RDeBerardinis Ralph JAzevedo Jorge EWarscheid Bettina - Peroxisomal biogenesis disorders (PBD) are autosomal recessive diseases caused by mutations in specific PEX genes that impair peroxisome formation, leading to multi-systemic failure. Symptoms vary, even in patients with variants in the same PEX gene. Our goal is to select PEX mutations and use Drosophila to model a severity spectrum based on genotype-phenotype correlations. Utilizing KozakGAL4 (KZ) cassettes, we replaced the coding sequence of Pex with a GAL4 driver, ideal for making 'humanized' flies in which human PEX can replace the fly loss. We generated Pex2KZ and Pex16KZ lines and assessed them in various behavior assays, confirming their severe phenotypes. We performed rescue with human reference, variant PEX2 and PEX16 alleles, and phenotypic rescue was observed when human PEX2Ref or PEX16Ref were expressed in Pex2KZ or Pex16KZ flies, respectively. We identified a severity spectrum for PEX2 and PEX16 alleles, with some missense mutations exhibiting severity comparable to truncations. Alleles linked to mild PBD showed partial rescue, while variants associated with atypical ataxia could fully rescue. Drosophila humanization is an effective method to study the range of severity of PBD. - Source: PubMed
Publication date: 2025/07/28
Gomez Vanessa AKanca OguzJangam Sharayu VSrivastav SaurabhAndrews Jonathan CWangler Michael F