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monoubiquitination of the N-terminal cysteine of peroxisome-associated PEX5 not only functions to recycle the peroxin back to the cytosol, but also serves as a quality control mechanism to eliminate peroxisomes with a defective protein import machinery
Demyelination in cerebellum and brain stem preceded major myelin loss in corpus callosum of Pex5 deficient mice.
interaction of PEX5 with catalase (show CAT Proteins) and PEX14 (show PEX14 Proteins)
Peroxisomes were selectively reconstituted in brain or liver of Pex5 knock-out mice, a model for Zellweger syndrome (show PEX1 Proteins), by tissue-selective overexpression of Pex5p. We found that both rescue strains exhibited a correction of the neuronal migration defect
these findings lend credit to the idea that inefficient catalase (show CAT Proteins) import, when coupled with the role of PEX5 as a redox-regulated import receptor, constitutes a cellular defense mechanism to combat oxidative insults of extra-peroxisomal origin.
TRIM37 (show TRIM37 Proteins)-mediated ubiquitylation stabilizes PEX5 and promotes peroxisomal matrix protein import, suggesting that mulibrey nanism is a new peroxisomal biogenesis disorder.
Data suggest that soluble/cytosolic PEX5 interacts with PEX14 (show PEX14 Proteins)/PEX13 (show PEX13 Proteins) complex, a model for the docking/translocation module (DTM) of the peroxisomal matrix protein translocon; PEX14 (show PEX14 Proteins)/PEX13 (show PEX13 Proteins) complex appears to function in peroxisomal membrane as large cavity into which cytosolic PEX5 can enter to release its cargo. (PEX (show PHEX Proteins) = peroxisomal biogenesis factor)
data reveal subpopulations of peroxisomes showing only weak colocalization between PEX14 (show PEX14 Proteins) and PEX5 or PEX11 but at the same time a clear compartmentalized organization. This compartmentalization, which was less evident in cases of strong colocalization, indicates dynamic protein reorganization linked to changes occurring in the peroxisomes.
our data suggest that insertion of the trimeric PEX5-PEX7 (show PEX7 Proteins)-PTS2 protein complex into the DTM is probably accompanied by conformational alterations in PEX5 to allow release of the PTS2 protein into the organelle matrix
Our data suggest that the functional polymorphism rs3814058C>T in 3'-UTR of PXR (show NR1I2 Proteins) may be a functional biomarker to predict risk of colorectal cancer
PEX5 encodes two isoforms, PEX5L & PEX5S, & a homozygous frame shift mutation c.722dupA (p.Val242Glyfs( *)33), located in the PEX5L-specific exon 9, results in loss of PEX5L only. Loss of PEX5L results in deficient import of PTS2-tagged proteins
bulky side chain within the recognition motif, which blocks contraction of the PEX5 binding cavity
Data show that ataxia-telangiectasia mutated (ATM (show ATM Proteins)) phosphorylates peroxisomal biogenesis factor 5 (PEX5) at serine 141 in response to reactive oxygen species.
ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulating PTS1 protein import
The product of this gene binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. Peroxins (PEXs) are proteins that are essential for the assembly of functional peroxisomes. The peroxisome biogenesis disorders (PBDs) are a group of genetically heterogeneous autosomal recessive, lethal diseases characterized by multiple defects in peroxisome function. The peroxisomal biogenesis disorders are a heterogeneous group with at least 14 complementation groups and with more than 1 phenotype being observed in cases falling into particular complementation groups. Although the clinical features of PBD patients vary, cells from all PBD patients exhibit a defect in the import of one or more classes of peroxisomal matrix proteins into the organelle. Defects in this gene are a cause of neonatal adrenoleukodystrophy (NALD), a cause of Zellweger syndrome (ZWS) as well as may be a cause of infantile Refsum disease (IRD). Alternatively spliced transcript variants encoding different isoforms have been identified.
peroxisome biogenesis factor 5
, PTS1 receptor
, peroxin 5
, peroxisomal C-terminal targeting signal import receptor
, peroxisomal targeting signal 1 receptor
, peroxisome receptor 1
, peroxisomal targeting signal 1 (SKL type) receptor
, peroxisomal targeting signal import receptor
, peroxisomal targeting signal receptor 1
, Peroxisomal C-terminal targeting signal import receptor
, Peroxisome receptor 1