An isoform of pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes.

@article{Braverman1998AnIO,
  title={An isoform of pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes.},
  author={Nancy E. Braverman and Gabriele Dodt and Steven J. Gould and David Valle},
  journal={Human molecular genetics},
  year={1998},
  volume={7 8},
  pages={
          1195-205
        }
}
Mutations in the peroxisome targeting signal (PTS) 1 receptor gene, PEX5 , are responsible for complementation group (CG) 2 of the peroxisome biogenesis disorders (PBD). Of the two reported patients in this CG, cells from PBD018 (homozygous for the missense mutation N489K) are defective in the import of PTS1 proteins into peroxisomes, as expected. However, cells from PBD005 (homozygous for the nonsense mutation R390ter) are defective in the import of both PTS1 and PTS2 proteins, suggesting that… 
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Disruption of the Interaction of the Longer Isoform of Pex5p, Pex5pL, with Pex7p Abolishes Peroxisome Targeting Signal Type 2 Protein Import in Mammals
TLDR
The results indicate that ZPG231 is the first cell mutant providing evidence that disruption of the Pex5pL-Pex7p interaction completely abolishes PTS2 import in mammals.
The Mammalian Peroxin Pex5pL, the Longer Isoform of the Mobile Peroxisome Targeting Signal (PTS) Type 1 Transporter, Translocates the Pex7p·PTS2 Protein Complex into Peroxisomes via Its Initial Docking Site, Pex14p*
TLDR
It is found that Pex5pL directly interacts with the PTS2 receptor Pex7p, carrying its cargo PTS2 protein in the cytosol, demonstrating that P Ex 5pL plays a pivotal role in peroxisomal PTS2 import.
The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5.
TLDR
The isolation and characterization of an Arabidopsis peroxin mutant, pex7-1, is described, which displays peroxisome-defective phenotypes including reduced PTS2 protein import, and it is demonstrated that the pex5-1 PTS1 receptor mutant, which contains a lesion in a domain conserved among PEX7-binding proteins from various organisms, is defective not in PTS1protein import, but rather in PTS2protein import.
Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins
TLDR
Oleate-inducible targeting of malate synthases into yeast peroxisomes is facilitated by the newly identified PTS1 receptor Pex9p, which exhibits a strong selectivity for these isoenzymes.
Functional Similarity between the Peroxisomal PTS2 Receptor Binding Protein Pex18p and the N-Terminal Half of the PTS1 Receptor Pex5p
TLDR
It is demonstrated, using different techniques, that in Saccharomyces cerevisiae Pex5p-N alone facilitates the import of the major matrix protein Fox1p and it is proposed that the auxiliary proteins of the PTS2 import pathway fulfill roles similar to those of the N-terminal half of Px5p in the PTS1 import pathway.
Intracellular Localization, Function, and Dysfunction of the Peroxisome-targeting Signal Type 2 Receptor, Pex7p, in Mammalian Cells*
TLDR
Cloned Chinese hamster (Cl) PEX7 encoding the PTS2 receptor is cloned, finding that nearly the full length of Pex7p, including all WD motifs, is required for its function.
Hsp70 regulates the interaction between the peroxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1.
TLDR
Hsp70 and ATP synergistically enhanced the binding of Pex5p to the C-terminal PTS1-containing part of AOx, implying that Px5p recognizes its cargo PTS1 protein by chaperone-assisted as well as energy-dependent mechanisms in vivo.
Pex 9 p is a novel yeast peroxisomal import receptor for PTS 1-proteins
TLDR
The existence of two distinct PTS1-receptors, in addition to two PTS2-dependent import routes, contributes to the adaptive metabolic capacity of peroxisomes in response to environmental changes and underlines the role of perxisomes as multi-purpose organelles.
Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients.
TLDR
It seems apparent that -AKL and -KANL are poorer variants of PTS1 and are likely to be more susceptible to effects of mutation of its receptor, Pex5p.
Quantitative analysis of peroxisomal targeting signal type-1 binding to wild-type and pathogenic mutants of Pex5p supports an affinity threshold for peroxisomal protein targeting.
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References

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Peroxisome Targeting Signal Type 1 (PTS1) Receptor Is Involved in Import of Both PTS1 and PTS2: Studies withPEX5-Defective CHO Cell Mutants
TLDR
A peroxisome-deficient CHO cell mutant, ZP139, was isolated and characterized, which was found to belong to human complementation group II, the same group as that of that of ZP105, which had a phenotypic deficiency in the import of peroxISomal targeting signal type 1 (PTS1) proteins.
Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders
TLDR
The cloned and sequenced human cDNA homologue (PTS1R) of the Pichia pastoris PAS8 gene, the PTS1 receptor, represents the only case in which the molecular basis of the protein-import deficiency in human peroxisomal disorders is understood.
The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor.
TLDR
It is concluded that Pxaaa1p plays a direct role in peroxisomal protein import and is required for PTS1 receptor activity.
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TLDR
It is shown that cells deficient in Pex13p are unable to import peroxisomal matrix proteins containing PTS1 and, surprisingly, also those containing PTS2, consistent with the existence of independent pathways for the integration of per oxisomal membrane proteins and for the translocation of peroxiomatic matrix proteins.
Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor
TLDR
Altered distribution or stability of the PTS1 receptor in all cells with a defect in PTS1 protein import implies that the genes mutated in these cell lines encode proteins with a direct role in peroxisomal protein import.
Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor
TLDR
It is concluded that Pex13p functions as a docking factor for the predominantly cytoplasmic PTS1 receptor and eliminates import of peroxisomal matrix proteins that contain either the type-1 or type-2 peroxISomal targeting signal but does not affect targeting and insertion of integral perox isomal membrane proteins.
Peb1p (Pas7p) is an intraperoxisomal receptor for the NH2-terminal, type 2, peroxisomal targeting sequence of thiolase: Peb1p itself is targeted to peroxisomes by an NH2-terminal peptide
TLDR
The results suggest that Peb1p (Pas7p) is an intraperoxisomal receptor for the type 2 peroxisome targeting signal.
The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene.
TLDR
Pas7p is the targeting signal‐specific receptor of thiolase in Saccharomyces cerevisiae and this observation suggests that in the human peroxisomal disorders characterized by an import defect for PTS2 proteins, a functional homologue of Pas7p may be impaired.
Isolation of the human PEX12 gene, mutated in group 3 of the peroxisome biogenesis disorders
TLDR
PEX12 expression restored peroxisomal protein import in fibroblasts from PBD patients of complement group 3 (CG3) and frameshift mutations in PEX12 were detected in two unrelated CG3 patients, demonstrating that mutations in pEX12 are responsible for CG3 of the PBD and that PEX 12 plays an essential role in peroxISomal matrix protein import.
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TLDR
The phenotypes of group I and IV cells provide the first evidence for differential import deficiencies in higher eukaryotes, analogous to those found in Saccharomyces cerevisiae peroxisome assembly mutants.
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