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Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans

Huang, C; Wagner-Valladolid, S; Stephens, AD; Jung, R; Poudel, C; Sinnige, T; Lechler, MC; ... David, DC; + view all (2019) Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans. Elife , 8 , Article e43059. 10.7554/eLife.43059. Green open access

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Abstract

Reduced protein homeostasis leading to increased protein instability is a common molecular feature of aging, but it remains unclear whether this is a cause or consequence of the aging process. In neurodegenerative diseases and other amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological aggregates in different tissues. More recently, widespread protein aggregation has been described during normal aging. Until now, an extensive characterization of the nature of age-dependent protein aggregation has been lacking. Here, we show that age-dependent aggregates are rapidly formed by newly synthesized proteins and have an amyloid-like structure resembling that of protein aggregates observed in disease. We then demonstrate that age-dependent protein aggregation accelerates the functional decline of different tissues in C. elegans. Together, these findings imply that amyloid-like aggregates contribute to the aging process and therefore could be important targets for strategies designed to maintain physiological functions in the late stages of life.

Type: Article
Title: Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans
Open access status: An open access version is available from UCL Discovery
DOI: 10.7554/eLife.43059
Publisher version: https://doi.org/10.7554/eLife.43059
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: C. elegans, cell biology, molecular biophysics, structural biology
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL
URI: https://discovery.ucl.ac.uk/id/eprint/10073408
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