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Nature Cell Biology (2026)
Paraspeckle condensates are membraneless nuclear organelles linked to stress responses and disease states. We demonstrate that paraspeckle assembly is tightly controlled by antagonism between TDP-43 and other paraspeckle proteins, through non-random distribution of TDP-43 binding sites on the scaffolding RNA NEAT1. Structural changes in NEAT1 or altered protein stoichiometry affect condensate formation, with implications for neurodegeneration.
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Nakagawa, S., Naganuma, T., Shioi, G. & Hirose, T. Paraspeckles are subpopulation-specific nuclear bodies that are not essential in mice. J. Cell Biol. 193, 31–39 (2011). This article reported limited NEAT1_2 expression and paraspeckle assembly in most mammalian tissues.
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An, H. et al. ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles. Acta Neuropathol. Commun. 7, 7 (2019). This paper reports defective paraspeckle assembly in an ALS subtype despite upregulation of NEAT1_2.
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This is a summary of: Hodgson, R. E. et al. Paraspeckle condensation is controlled via TDP-43 polymerization and linked to neuroprotection. Nat. Cell Biol. https://doi.org/10.1038/s41556-026-01895-y (2026).
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Linking TDP-43-regulated paraspeckle condensation to neuroprotection. Nat Cell Biol (2026). https://doi.org/10.1038/s41556-026-01932-w
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DOI: https://doi.org/10.1038/s41556-026-01932-w
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Nature Cell Biology (Nat Cell Biol)
ISSN 1476-4679 (online)
ISSN 1465-7392 (print)
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