ArticleMolecular biology of the cell2010
Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Transgenic Overexpression of the Disordered Prion Protein N1 Fragment in Mice Does Not Protect Against Neurodegenerative Diseases Due to Impaired ER Translocation.Molecular neurobiology · 2020Article
- Building an Artificial Stem Cell Niche: Prerequisites for Future 3D-Formation of Inner Ear Structures-Toward 3D Inner Ear Biotechnology.Anatomical record (Hoboken, N.J. : 2007) · 2020Review
- Article
- Mutant-selective topologic conversion facilitates selective degradation of a pathogenic prion isoform.Cell death and differentiation · 2020Article
- A technique for delineating the unfolding requirements for substrate entry into retrotranslocons during endoplasmic reticulum-associated degradation.The Journal of biological chemistry · 2019Article
- Recognition and Degradation of Mislocalized Proteins in Health and Disease.Cold Spring Harbor perspectives in biology · 2019Review
- Polarity signaling ensures epidermal homeostasis by coupling cellular mechanics and genomic integrity.Nature communications · 2019Article
- Regenerative therapy based on miRNA-302 mimics for enhancing host recovery from pneumonia caused byProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis.The Journal of cell biology · 2018Article
- The sole introduction of two single-point mutations establishes glycerol utilization inBiotechnology for biofuels · 2017Article
- Comparative Haploid Genetic Screens Reveal Divergent Pathways in the Biogenesis and Trafficking of Glycophosphatidylinositol-Anchored Proteins.Cell reports · 2015Article
- Shedding light on prion disease.Prion · 2015Article
- CD4 and BST-2/tetherin proteins retro-translocate from endoplasmic reticulum to cytosol as partially folded and multimeric molecules.The Journal of biological chemistry · 2014Article
- Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion protein.Neural regeneration research · 2013Review
- Review
- Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.The Journal of biological chemistry · 2012Article
- Understanding integration of α-helical membrane proteins: the next steps.Trends in biochemical sciences · 2012Article
- Human prion protein binds Argonaute and promotes accumulation of microRNA effector complexes.Nature structural & molecular biology · 2012Article
- Article
- Protein targeting and degradation are coupled for elimination of mislocalized proteins.Nature · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Proteins are often made in more than one form, with alternate versions sometimes residing in different cellular compartments than the primary species. The mammalian prion protein (PrP), a cell surface GPI-anchored protein, is a particularly noteworthy example for which minor cytosolic and transmembrane forms have been implicated in disease pathogenesis. To study these minor species, we used a selective labeling strategy in which spatially restricted expression of a biotinylating enzyme was combined with asymmetric engineering of the cognate acceptor sequence into PrP. Using this method, we could show that even wild-type PrP generates small amounts of the (Ctm)PrP transmembrane form. Selective detection of (Ctm)PrP allowed us to reveal its N-terminal processing, long half-life, residence in both intracellular and cell surface locations, and eventual degradation in the lysosome. Surprisingly, some human disease-causing mutants in PrP selectively stabilized (Ctm)PrP, revealing a previously unanticipated mechanism of (Ctm)PrP up-regulation that may contribute to disease. Thus, spatiotemporal tagging has uncovered novel aspects of normal and mutant PrP metabolism and should be readily applicable to the analysis of minor topologic isoforms of other proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.