ArticlePloS one2013
The ZIP5 ectodomain co-localizes with PrP and may acquire a PrP-like fold that assembles into a dimer.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Functional characterization of SLC39 family members ZIP5 and ZIP10 in overexpressing HEK293 cells reveals selective copper transport activity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Probing the origin of prion protein misfolding via reconstruction of ancestral proteins.Protein science : a publication of the Protein Society · 2022Article
- Neurometals in the Pathogenesis of Prion Diseases.International journal of molecular sciences · 2021Review
- Molecular Basis of Zinc-Dependent Endocytosis of Human ZIP4 Transceptor.Cell reports · 2020Article
- Review
- Zinc Transporter Proteins.Neurochemical research · 2018Review
- A ZIP6-ZIP10 heteromer controls NCAM1 phosphorylation and integration into focal adhesion complexes during epithelial-to-mesenchymal transition.Scientific reports · 2017Article
- Review
- Zinc transporter ZIP10 forms a heteromer with ZIP6 which regulates embryonic development and cell migration.The Biochemical journal · 2016Article
- Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.Nature communications · 2016Article
- Article
- SLC39A5 mutations interfering with the BMP/TGF-β pathway in non-syndromic high myopia.Journal of medical genetics · 2014Article
- Genome wide identification, phylogeny and expression of zinc transporter genes in common carp.PloS one · 2014Article
- Zinc transporters and their functional integration in mammalian cells.The Journal of biological chemistryReview
- The emerging role of zinc transporters in cellular homeostasis and cancer.Signal transduction and targeted therapyArticle
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Authors and funding
14 authors.
Funding
Abstract
The cellular prion protein (PrP(C)) was recently observed to co-purify with members of the LIV-1 subfamily of ZIP zinc transporters (LZTs), precipitating the surprising discovery that the prion gene family descended from an ancestral LZT gene. Here, we compared the subcellular distribution and biophysical characteristics of LZTs and their PrP-like ectodomains. When expressed in neuroblastoma cells, the ZIP5 member of the LZT subfamily was observed to be largely directed to the same subcellular locations as PrP(C) and both proteins were seen to be endocytosed through vesicles decorated with the Rab5 marker protein. When recombinantly expressed, the PrP-like domain of ZIP5 could be obtained with yields and levels of purity sufficient for structural analyses but it tended to aggregate, thereby precluding attempts to study its structure. These obstacles were overcome by moving to a mammalian cell expression system. The subsequent biophysical characterization of a homogeneous preparation of the ZIP5 PrP-like ectodomain shows that this protein acquires a dimeric, largely globular fold with an α-helical content similar to that of mammalian PrP(C). The use of a mammalian cell expression system also allowed for the expression and purification of stable preparations of Takifugu rubripes PrP-1, thereby overcoming a key hindrance to high-resolution work on a fish PrP(C).
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