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Int. J. Mol. Sci. 2015, 16(3), 6076-6092; doi:10.3390/ijms16036076

Conformational Analysis of Misfolded Protein Aggregation by FRET and Live-Cell Imaging Techniques

1
Laboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, Japan
2
Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Herbert Schneckenburger
Received: 3 February 2015 / Revised: 5 March 2015 / Accepted: 11 March 2015 / Published: 16 March 2015
(This article belongs to the Special Issue Förster Resonance Energy Transfer (FRET) 2015)
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Abstract

Cellular homeostasis is maintained by several types of protein machinery, including molecular chaperones and proteolysis systems. Dysregulation of the proteome disrupts homeostasis in cells, tissues, and the organism as a whole, and has been hypothesized to cause neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS) and Huntington’s disease (HD). A hallmark of neurodegenerative disorders is formation of ubiquitin-positive inclusion bodies in neurons, suggesting that the aggregation process of misfolded proteins changes during disease progression. Hence, high-throughput determination of soluble oligomers during the aggregation process, as well as the conformation of sequestered proteins in inclusion bodies, is essential for elucidation of physiological regulation mechanism and drug discovery in this field. To elucidate the interaction, accumulation, and conformation of aggregation-prone proteins, in situ spectroscopic imaging techniques, such as Förster/fluorescence resonance energy transfer (FRET), fluorescence correlation spectroscopy (FCS), and bimolecular fluorescence complementation (BiFC) have been employed. Here, we summarize recent reports in which these techniques were applied to the analysis of aggregation-prone proteins (in particular their dimerization, interactions, and conformational changes), and describe several fluorescent indicators used for real-time observation of physiological states related to proteostasis. View Full-Text
Keywords: proteostasis; neurodegenerative disease; protein aggregation; protein misfolding; SOD1; FRET; FCS; fluorescent protein proteostasis; neurodegenerative disease; protein aggregation; protein misfolding; SOD1; FRET; FCS; fluorescent protein
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kitamura, A.; Nagata, K.; Kinjo, M. Conformational Analysis of Misfolded Protein Aggregation by FRET and Live-Cell Imaging Techniques. Int. J. Mol. Sci. 2015, 16, 6076-6092.

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