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• W2071113961 abstract "A large number of mutations in the human PLP1 gene lead to abnormal myelination and oligodendrocyte death in Pelizaeus-Merzbacher disease (PMD). Here we show that a major subgroup of PMD mutations that map into the extracellular loop region of PLP/DM20 leads to the failure of oligodendrocytes to form the correct intramolecular disulfide bridges. This leads to abnormal protein cross-links and endoplasmic reticulum retention and activates the unfolded protein response. Importantly, surface expression of mutant PLP/DM20 can be restored and the unfolded protein response can be reverted by the removal of two cysteines. Thus, covalent protein cross-links emerge as a cause, rather than as a consequence, of endoplasmic reticulum retention." @default.
• W2071113961 created "2016-06-24" @default.
• W2071113961 creator A5038465445 @default.
• W2071113961 creator A5061733465 @default.
• W2071113961 date "2007-11-06" @default.
• W2071113961 modified "2023-10-17" @default.
• W2071113961 title "A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus–Merzbacher disease" @default.
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• W2071113961 doi "https://doi.org/10.1073/pnas.0704975104" @default.
• W2071113961 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2077047" @default.
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