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Protein aggregation in neurodegenerative disease: the nucleolar connection

  • Received: 14 May 2015 Accepted: 13 July 2015 Published: 24 July 2015
  • Protein- and sometimes RNA-containing aggregates are a hallmark of many age-related neurodegenerative diseases. Aggregate depositions can be cytoplasmic, nuclear and even extracellular. This article focuses on nuclear aggregation and the potential role of a specific compartment—the nucleolus, in the process. The nucleolus is a formation site of nucleolar aggresomes—protein and RNA aggregates formed in vitro by hampered proteasome function. Whether the nucleolar aggresomes are connected to nuclear aggregation involved in certain neurodegenerative diseases is an intriguing question for future studies. In addition, recent evidence connecting aggregation and aggregate sorting in the cytoplasm to membrane-enveloped organelles, namely ER and mitochondria, raises the question whether nuclear aggregation and aggregate positioning is controlled by different mechanisms or by the only membrane available—the nuclear membrane.

    Citation: Leena Latonen. Protein aggregation in neurodegenerative disease: the nucleolar connection[J]. AIMS Molecular Science, 2015, 2(3): 324-331. doi: 10.3934/molsci.2015.3.324

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  • Protein- and sometimes RNA-containing aggregates are a hallmark of many age-related neurodegenerative diseases. Aggregate depositions can be cytoplasmic, nuclear and even extracellular. This article focuses on nuclear aggregation and the potential role of a specific compartment—the nucleolus, in the process. The nucleolus is a formation site of nucleolar aggresomes—protein and RNA aggregates formed in vitro by hampered proteasome function. Whether the nucleolar aggresomes are connected to nuclear aggregation involved in certain neurodegenerative diseases is an intriguing question for future studies. In addition, recent evidence connecting aggregation and aggregate sorting in the cytoplasm to membrane-enveloped organelles, namely ER and mitochondria, raises the question whether nuclear aggregation and aggregate positioning is controlled by different mechanisms or by the only membrane available—the nuclear membrane.


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