ALS/FTD-associated mutation in cyclin F inhibits ER-Golgi trafficking, inducing ER stress, ERAD and Golgi fragmentation

Authors

Audrey M.G. Ragagnin, The Faculty of Medicine, Health and Human Sciences
Vinod Sundaramoorthy, The Faculty of Medicine, Health and Human Sciences
Fabiha Farzana, The Faculty of Medicine, Health and Human Sciences
Shashi Gautam, The Faculty of Medicine, Health and Human Sciences
Sayanthooran Saravanabavan, The Faculty of Medicine, Health and Human Sciences
Zeinab Takalloo, The Faculty of Medicine, Health and Human Sciences
Prachi Mehta, The Faculty of Medicine, Health and Human Sciences
Dzung Do-Ha, University of Wollongong
Sonam Parakh, The Faculty of Medicine, Health and Human Sciences
Sina Shadfar, The Faculty of Medicine, Health and Human Sciences
Julie Hunter, The Faculty of Medicine, Health and Human Sciences
Marta Vidal, The Faculty of Medicine, Health and Human Sciences
Cyril J. Jagaraj, The Faculty of Medicine, Health and Human Sciences
Mariana Brocardo, The Faculty of Medicine, Health and Human Sciences
Anna Konopka, The Faculty of Medicine, Health and Human Sciences
Shu Yang, The Faculty of Medicine, Health and Human Sciences
Stephanie L. Rayner, The Faculty of Medicine, Health and Human Sciences
Kelly L. Williams, The Faculty of Medicine, Health and Human Sciences
Ian P. Blair, The Faculty of Medicine, Health and Human Sciences
Roger S. Chung, The Faculty of Medicine, Health and Human Sciences
Albert Lee, The Faculty of Medicine, Health and Human Sciences
Lezanne Ooi, University of Wollongong
Julie D. Atkin, The Faculty of Medicine, Health and Human Sciences

Publication Name

Scientific Reports

Abstract

Amyotrophic lateral sclerosis (ALS) is a severely debilitating neurodegenerative condition that is part of the same disease spectrum as frontotemporal dementia (FTD). Mutations in the CCNF gene, encoding cyclin F, are present in both sporadic and familial ALS and FTD. However, the pathophysiological mechanisms underlying neurodegeneration remain unclear. Proper functioning of the endoplasmic reticulum (ER) and Golgi apparatus compartments is essential for normal physiological activities and to maintain cellular viability. Here, we demonstrate that ALS/FTD-associated variant cyclin FS621G inhibits secretory protein transport from the ER to Golgi apparatus, by a mechanism involving dysregulation of COPII vesicles at ER exit sites. Consistent with this finding, cyclin FS621G also induces fragmentation of the Golgi apparatus and activates ER stress, ER-associated degradation, and apoptosis. Induction of Golgi fragmentation and ER stress were confirmed with a second ALS/FTD variant cyclin FS195R, and in cortical primary neurons. Hence, this study provides novel insights into pathogenic mechanisms associated with ALS/FTD-variant cyclin F, involving perturbations to both secretory protein trafficking and ER-Golgi homeostasis.

Open Access Status

This publication is not available as open access

Volume

13

Issue

1

Article Number

20467

Funding Number

10305133

Funding Sponsor

National Institutes of Health

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Link to publisher version (DOI)

http://dx.doi.org/10.1038/s41598-023-46802-9