Protein aggregation in neurodegenerative disease: the nucleolar connection

Leena Latonen; Leena Latonen

doi:10.3934/molsci.2015.3.324

AIMS Molecular Science

2015, Volume 2, Issue 3: 324-331. doi: 10.3934/molsci.2015.3.324

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Protein aggregation in neurodegenerative disease: the nucleolar connection

Leena Latonen ^,

Institute of Biosciences and Medical Technology, University of Tampere, FI-33014, Finland

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.
- neurodegenerative disease,
- nucleolus,
- proteasome,
- aggresome,
- aggregation
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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Abstract

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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