ArticleThe Journal of biological chemistry2017
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- CPEB3 selectively inhibits α-synuclein aggregation without modulating TDP-43 pathology.FEBS letters · 2026Article
- pH Sensitivity of the SERF1a Conformational Ensemble.ACS omega · 2026Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.bioRxiv : the preprint server for biology · 2024Article
- Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2.Biomolecular NMR assignments · 2024Article
- Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation.Nucleic acids research · 2024Article
- Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation.bioRxiv : the preprint server for biology · 2024Article
- Chaperones vs. oxidative stress in the pathobiology of ischemic stroke.Frontiers in molecular neuroscience · 2024Review
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain.Life science alliance · 2023Article
- The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation.The EMBO journal · 2021Article
- The contribution of electrostatics to hydrogen exchange in the unfolded protein state.Biophysical journal · 2021Article
- NMR spectroscopy charges into protein surface electrostatics.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel knockout mouse for the small EDRK-rich factor 2 (Serf2) showing developmental and other deficits.Mammalian genome : official journal of the International Mammalian Genome Society · 2021Article
- Regulation of Age-Related Protein Toxicity.Frontiers in cell and developmental biology · 2021Review
- SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation.Chemistry and physics of lipids · 2019Article
- The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions.Scientific reports · 2019Article
- α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies.Scientific reports · 2018Article
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9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Aberrant protein aggregation underlies a variety of age-related neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. Little is known, however, about the molecular mechanisms that modulate the aggregation process in the cellular environment. Recently, MOAG-4/SERF has been identified as a class of evolutionarily conserved proteins that positively regulates aggregate formation. Here, by using nuclear magnetic resonance (NMR) spectroscopy, we examine the mechanism of action of MOAG-4 by characterizing its interaction with α-synuclein (α-Syn). NMR chemical shift perturbations demonstrate that a positively charged segment of MOAG-4 forms a transiently populated α-helix that interacts with the negatively charged C terminus of α-Syn. This process interferes with the intramolecular interactions between the N- and C-terminal regions of α-Syn, resulting in the protein populating less compact forms and aggregating more readily. These results provide a compelling example of the complex competition between molecular and cellular factors that protect against protein aggregation and those that promote it.
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