ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007
Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. 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, 21 citations in OpenAlex.
- A point mutation in GPI-attachment signal peptide accelerates the development of prion disease.Acta neuropathologica · 2023Article
- Cellular prion protein is present in mitochondria of healthy mice.Scientific reports · 2017Article
- Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Human molecular genetics · 2016Article
- Yeast as a tool for studying proteins of the Bcl-2 family.Microbial cell (Graz, Austria) · 2015Review
- Cyclin-dependent kinase 5 phosphorylation of familial prion protein mutants exacerbates conversion into amyloid structure.The Journal of biological chemistry · 2015Article
- Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer.Breast cancer research : BCR · 2013Article
- Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival.The Journal of biological chemistry · 2012Article
- Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Journal of molecular biology · 2010Article
- Loss of anti-Bax function in Gerstmann-Sträussler-Scheinker syndrome-associated prion protein mutants.PloS one · 2009Article
- The consequences of pathogenic mutations to the human prion protein.Protein engineering, design & selection : PEDS · 2009Review
- Phosphorylation of prion protein at serine 43 induces prion protein conformational change.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Cytoplasmic prion protein induces forebrain neurotoxicity.Biochimica et biophysica acta · 2009Article
- Helix 3 is necessary and sufficient for prion protein's anti-Bax function.Journal of neurochemistry · 2009Article
- Cytosolic prion protein is the predominant anti-Bax prion protein form: exclusion of transmembrane and secreted prion protein forms in the anti-Bax function.Biochimica et biophysica acta · 2008Article
- Prion protein lacks robust cytoprotective activity in cultured cells.Molecular neurodegeneration · 2008Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prion protein (PrP) inhibits the activation of proapoptotic Bax in primary human neurons and MCF-7 cells. Because neuronal apoptosis occurs in human prion diseases, here we examine the anti-Bax function of familial PrP mutants. All Creutzfeldt-Jakob disease and fatal familial insomnia-associated prion protein mutations partially or completely lose the anti-Bax function in human neurons and, except for A117V and V203I, in MCF-7 cells. The ability of the mutants to protect against Bax-mediated cell death is divided into three groups: (1) group I, retention of anti-Bax function in both the Val129 and Met129 mutants; (2) group II, retention of anti-Bax function only in Val129 mutants; and (3) group III, reduction or no anti-Bax function in Val129 and Met129 mutants. The loss of anti-Bax function in these PrP mutants correlates completely with a significant decrease in the production of cytosolic PrP, a form of PrP shown previously to have anti-Bax function in human neurons. Cotransfection of the full-length PrP mutants with wild-type or mutant cytosolic PrP, but not with wild type full-length PrP, rescues the anti-Bax function of PrP. The results show that the failure of PrP mutants to produce cytosolic PrP is responsible for the loss of anti-Bax function and that the effect of the PrP mutants is dominant over wild-type PrP. Furthermore, these results imply that misfolded PrP that escapes retrotranslocation could accumulate at the cell surface and cause neuronal dysfunction.
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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.