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• W2972300128 endingPage "708" @default.
• W2972300128 startingPage "693" @default.
• W2972300128 abstract "Neurons have several unique membraneless compartments generated by phase separation, including the postsynaptic density and elements of the presynapse. Many neurodegenerative-disease associated proteins are found in MLOs and/or are capable of phase separation; several hypotheses link membraneless compartments to toxic aggregates observed in disease. PTMs, including phosphorylation, methylation, and addition of poly(ADP-ribose), are potential therapeutic targets for modulating phase separation and aggregation. Further research will be necessary, however, to fully understand the effects of PTMs on MLOs and to develop targeted therapeutics. Neurons require unique subcellular compartmentalization to function efficiently. Formed from proteins and RNAs through liquid–liquid phase separation, membraneless organelles (MLOs) have emerged as one way in which cells form distinct, specialized compartments in the absence of lipid membranes. We first discuss MLOs that are common to many cell types as well as those that are specific to neurons. Interestingly, many proteins associated with neurodegenerative disease are found in MLOs, particularly in stress and transport granules. We next review possible links between neurodegeneration and MLOs, and the hypothesis that the protein and RNA inclusions formed in disease are related to the functional complexes occurring inside these MLOs. Finally, we discuss the hypothesis that protein post-translational modifications (PTMs), which can alter phase separation, can modulate MLO formation and provide potential new therapeutic strategies for currently untreatable neurodegenerative diseases. Neurons require unique subcellular compartmentalization to function efficiently. Formed from proteins and RNAs through liquid–liquid phase separation, membraneless organelles (MLOs) have emerged as one way in which cells form distinct, specialized compartments in the absence of lipid membranes. We first discuss MLOs that are common to many cell types as well as those that are specific to neurons. Interestingly, many proteins associated with neurodegenerative disease are found in MLOs, particularly in stress and transport granules. We next review possible links between neurodegeneration and MLOs, and the hypothesis that the protein and RNA inclusions formed in disease are related to the functional complexes occurring inside these MLOs. Finally, we discuss the hypothesis that protein post-translational modifications (PTMs), which can alter phase separation, can modulate MLO formation and provide potential new therapeutic strategies for currently untreatable neurodegenerative diseases. a physical phenomenon where (in the case of cells) proteins, RNAs, and other biomolecules demix from the surrounding mixture and form a distinct liquid phase within the liquid of the nucleus/cytoplasm (or surrounding solution); there is evidence for LLPS both biochemically and within cells. distinct puncta observed in cells that are not surrounded by a phospholipid membrane; their formation is thought to be mediated by phase separation from the surrounding liquid. a chemical signal covalently added to a protein by specific enzymes that catalyze the reaction; there are distinct enzymes that remove the chemical modification. a punctate structure observed in cells. Although their existence has been known for decades, more recently they have been recognized to be MLOs. Most RNA/RNP granules contain both RNAs and RNPs. the noncovalent interaction between π (i.e., sp2 hybridized) molecular orbitals of chemical groups, including those found in proteins. This interaction may include the stacking of two aromatic amino acids and contacts formed by the peptide bond region of amino acids. This interaction contributes to the phase separation of many disordered proteins, especially those enriched in π orbital-containing residues." @default.
• W2972300128 created "2019-09-12" @default.
• W2972300128 creator A5003043392 @default.
• W2972300128 creator A5077689800 @default.
• W2972300128 date "2019-10-01" @default.
• W2972300128 modified "2023-10-15" @default.
• W2972300128 title "Physiological, Pathological, and Targetable Membraneless Organelles in Neurons" @default.
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