The deubiquitination of the PTS1-import receptor Pex5p is required for peroxisomal matrix protein import

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Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling

Pex5p, which is the import receptor for peroxisomal matrix proteins harboring a type I signal sequence (PTS1), is mono- and polyubiquitinated in Saccharomyces cerevisiae. We identified Pex5p as a molecular target for Pex4p-dependent monoubiquitination and demonstrated that either poly- or monoubiquitination of the receptor is required for the ATP-dependent release of the protein from the peroxi...

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Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import.

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Ubiquitination of mammalian Pex5p, the peroxisomal import receptor.

Protein translocation across the peroxisomal membrane requires the concerted action of numerous peroxins. One central component of this machinery is Pex5p, the cycling receptor for matrix proteins. Pex5p recognizes newly synthesized proteins in the cytosol and promotes their translocation across the peroxisomal membrane. After this translocation step, Pex5p is recycled back into the cytosol to ...

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

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 ...

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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

PEX5 encodes the type-1 peroxisomal targeting signal (PTS1) receptor, one of at least 15 peroxins required for peroxisome biogenesis. Pex5p has a bimodal distribution within the cell, mostly cytosolic with a small amount bound to peroxisomes. This distribution indicates that Pex5p may function as a cycling receptor, a mode of action likely to require interaction with additional peroxins. Loss o...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

سال: 2019

ISSN: 0167-4889

DOI: 10.1016/j.bbamcr.2018.11.002