ArticleThe Biochemical journal2002
Functional studies on human Pex7p: subcellular localization and interaction with proteins containing a peroxisome-targeting signal type 2 and other peroxins.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Import mechanism of peroxisomal proteins with an N-terminal signal sequence.Nature cell biology · 2025Article
- Article
- Mechanistic insights into PTS2-mediated peroxisomal protein import: the co-receptor PEX5L drastically increases the interaction strength between the cargo protein and the receptor PEX7.The Journal of biological chemistry · 2015Article
- Redox-regulated cargo binding and release by the peroxisomal targeting signal receptor, Pex5.The Journal of biological chemistry · 2013Article
- Proteomic analysis reveals that the Rab GTPase RabE1c is involved in the degradation of the peroxisomal protein receptor PEX7 (peroxin 7).The Journal of biological chemistry · 2013Article
- Structural requirements for interaction of peroxisomal targeting signal 2 and its receptor PEX7.The Journal of biological chemistry · 2011Article
- Peroxisome matrix and membrane protein biogenesis.IUBMB life · 2009Review
- Identification of a novel PEX14 mutation in Zellweger syndrome.BMJ case reports · 2009Article
- Localization of the pre-squalene segment of the isoprenoid biosynthetic pathway in mammalian peroxisomes.Histochemistry and cell biology · 2007Article
- Pex7p translocates in and out of peroxisomes in Saccharomyces cerevisiae.The Journal of cell biology · 2004Article
- Peroxisome biogenesis and the role of protein import.Journal of cellular and molecular medicineReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pex7p is a WD40-containing protein involved in peroxisomal import of proteins containing an N-terminal peroxisome-targeting signal (PTS2). The interaction of human recombinant Pex7p expressed in different hosts/systems with its PTS2 ligand and other peroxins was analysed using various experimental approaches. Specific binding of human Pex7p to PTS2 could be demonstrated only when Pex7p was formed in vitro by a coupled transcription/translation system or synthesized in vivo in Chinese hamster ovary K1 cells transfected with a construct coding for a Pex7p-green fluorescent protein (GFP) fusion protein. Apparently, no cofactors are required and only monomeric Pex7p binds to PTS2. The interaction is reduced upon cysteine alkylation and is impaired upon truncation of the N-terminus of Pex7p. Interaction of Pex7p with other peroxins could not be demonstrated in bacterial or yeast two-hybrid screens, or in pull-down binding assays. The GFP fusion proteins, tagged at either the N- or C-terminus, were able to restore PTS2 import in rhizomelic chondrodysplasia punctata fibroblasts, and Pex7p-GFP was located both in the lumen of peroxisomes and in the cytosol.
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