ArticleProceedings of the National Academy of Sciences of the United States of America2005
Disease-associated mutations cause premature oligomerization of myelin proteolipid protein in the endoplasmic reticulum.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- Protein Self-Interaction in Cellular Function and Network Evolution: Molecular Mechanisms, AI-Driven Insights, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- Review
- Molecular insights into the comorbidity of vitamin K-dependent clotting factor deficiency and chondrodysplasia punctata.Journal of thrombosis and haemostasis : JTH · 2025Article
- Alterations in oligodendrocyte transcriptional networks reveal region-specific vulnerabilities to neurological disease.iScience · 2023Article
- Human myelin proteolipid protein structure and lipid bilayer stacking.Cellular and molecular life sciences : CMLS · 2022Article
- Membrane orientation and oligomerization of the melanocortin receptor accessory protein 2.The Journal of biological chemistry · 2020Article
- Drug screening for Pelizaeus-Merzbacher disease by quantifying the total levels and membrane localization of PLP1.Molecular genetics and metabolism reports · 2019Article
- Article
- Neurogenetics of Pelizaeus-Merzbacher disease.Handbook of clinical neurology · 2018Review
- Cellular Pathology of Pelizaeus-Merzbacher Disease Involving Chaperones Associated with Endoplasmic Reticulum Stress.Frontiers in molecular biosciences · 2017Review
- Novel molecular insights into the critical role of sulfatide in myelin maintenance/function.Journal of neurochemistry · 2016Article
- Identification of GPM6A and GPM6B as potential new human lymphoid leukemia-associated oncogenes.Cellular oncology (Dordrecht, Netherlands) · 2014Article
- Mutation of sec63 in zebrafish causes defects in myelinated axons and liver pathology.Disease models & mechanisms · 2013Article
- Misalignment of PLP/DM20 transmembrane domains determines protein misfolding in Pelizaeus-Merzbacher disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- A mutation in the mouse Amelx tri-tyrosyl domain results in impaired secretion of amelogenin and phenocopies human X-linked amelogenesis imperfecta.Human molecular genetics · 2010Article
- Computational Epigenetics: the new scientific paradigm.Bioinformation · 2010Article
- Differences in endoplasmic-reticulum quality control determine the cellular response to disease-associated mutants of proteolipid protein.Journal of cell science · 2009Article
- Endoplasmic reticulum stress in disorders of myelinating cells.Nature neuroscience · 2009Review
- A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The role of neuronal complexes in human X-linked brain diseases.American journal of human genetics · 2007Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pelizaeus-Merzbacher disease (PMD) is a dysmyelinating disease caused by mutations, deletions, or duplications of the proteolipid protein (PLP) gene. Mutant forms of PLP are retained in the endoplasmic reticulum (ER), and the resulting accumulation of mutant protein is thought to be a direct cause of oligodendrocyte cell death, which is the primary clinical feature of PMD. The molecular mechanisms underlying the toxicity of mutant PLP are however currently unknown. We report here that PMD-linked mutations of PLP are associated with the accelerated assembly of the protein into stable homooligomers that resemble mature, native PLP. Thus although WT PLP forms stable oligomers after an extended maturation period, most likely at the cell surface, mutant forms of PLP rapidly assemble into such oligomers at the ER. Using PLP mutants associated with diseases of varying severity, we show that the formation of stable oligomers correlates with the development of PMD. Based on these findings, we propose that the premature oligomerization of PLP in the ER of oligodendrocytes contributes to the pathology of PMD.
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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.