Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell

S Polling; YF Mok; YM Ramdzan; BJ Turner; JJ Yerbury; AF Hill; DM Hatters

Journal article

Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell

S Polling, YF Mok, YM Ramdzan, BJ Turner, JJ Yerbury, AF Hill, DM Hatters

Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2014

DOI: 10.1074/jbc.M113.520189

Abstract

Background: Protein aggregation is associated with neurodegenerative diseases. Results:Wedefined how the oligomeric state of disease-relevant mutant protein and homopolypeptides relate to clustering into inclusion subtypes IPOD and JUNQ. Conclusion: JUNQ protein and homopolypeptides relate to constitutively disrupted oligomeric states irrespective of inclusion formation. Significance: JUNQ inclusions may arise by cellular failure in degradation of abnormal oligomeric states. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

University of Melbourne Researchers

Yee Foong Mok Author

Bradley Turner Author

Danny M Hatters Author

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Grants

Funding Acknowledgements

This work was supported by Australian Research Council (ARC) Discovery Grant DP120102763 and ARC Future Fellowship Grant FT120100039 (to D. M. H.), and ARC Future Fellowship Grant FT100100560 (to A. F. H.).