ArticleThe Journal of cell biology1999
PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 150 citations in OpenAlex.
- Polyunsaturated fatty acid metabolism in the retinal pigment epithelium and its association with outer retinal disease.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Review
- Structural basis of receptor retro-translocation in peroxisomal protein import.bioRxiv : the preprint server for biology · 2026Article
- Article
- A founder mutation in PEX12 among Egyptian patients in peroxisomal biogenesis disorder.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2021Article
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Expanding the spectrum of PEX10-related peroxisomal biogenesis disorders: slowly progressive recessive ataxia.Journal of neurology · 2016Article
- Evolutionary loss of peroxisomes--not limited to parasites.Biology direct · 2015Article
- A novel mutation in the PEX12 gene causing a peroxisomal biogenesis disorder.Molecular biology reports · 2015Article
- Peripheral nervous system defects in a mouse model for peroxisomal biogenesis disorders.Developmental biology · 2014Article
- AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import.The Journal of biological chemistry · 2014Article
- Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulate PTS1 protein import.The Journal of biological chemistry · 2014Article
- The exportomer: the peroxisomal receptor export machinery.Cellular and molecular life sciences : CMLS · 2013Review
- Role of peroxisomes in the biosynthesis and secretion of β-lactams and other secondary metabolites.Journal of industrial microbiology & biotechnology · 2012Review
- Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2, and PEX12 in peroxisome formation and matrix protein import.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Pex2 and pex12 function as protein-ubiquitin ligases in peroxisomal protein import.Molecular and cellular biology · 2009Article
- Identification of novel mutations and sequence variation in the Zellweger syndrome spectrum of peroxisome biogenesis disorders.Human mutation · 2009Article
- Characterization of glycosomal RING finger proteins of trypanosomatids.Experimental parasitology · 2007Article
- A novel PEX12 mutation identified as the cause of a peroxisomal biogenesis disorder with mild clinical phenotype, mild biochemical abnormalities in fibroblasts and a mosaic catalase immunofluorescence pattern, even at 40 degrees C.Journal of human genetics · 2007Article
- Proteomics of the peroxisome.Biochimica et biophysica acta · 2006Review
- Two independent pathways traffic the intraperoxisomal peroxin PpPex8p into peroxisomes: mechanism and evolutionary implications.Molecular biology of the cell · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxisomal matrix protein import requires PEX12, an integral peroxisomal membrane protein with a zinc ring domain at its carboxy terminus. Mutations in human PEX12 result in Zellweger syndrome, a lethal neurological disorder, and implicate the zinc ring domain in PEX12 function. Using two-hybrid studies, blot overlay assays, and coimmunoprecipitation experiments, we observed that the zinc-binding domain of PEX12 binds both PEX5, the PTS1 receptor, and PEX10, another integral peroxisomal membrane protein required for peroxisomal matrix protein import. Furthermore, we identified a patient with a missense mutation in the PEX12 zinc-binding domain, S320F, and observed that this mutation reduces the binding of PEX12 to PEX5 and PEX10. Overexpression of either PEX5 or PEX10 can suppress this PEX12 mutation, providing genetic evidence that these interactions are biologically relevant. PEX5 is a predominantly cytoplasmic protein and previous PEX5-binding proteins have been implicated in docking PEX5 to the peroxisome surface. However, we find that loss of PEX12 or PEX10 does not reduce the association of PEX5 with peroxisomes, demonstrating that these peroxins are not required for receptor docking. These and other results lead us to propose that PEX12 and PEX10 play direct roles in peroxisomal matrix protein import downstream of the receptor docking event.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.