Loss of FIC-1-mediated AMPylation activates the UPRER and upregulates cytosolic HSP70 chaperones to suppress polyglutamine toxicity.
Targeted regulation of cellular proteostasis machinery represents a promising strategy for the attenuation of pathological protein aggregation. Recent work suggests that the unfolded protein response in the endoplasmic reticulum (UPRER) directly regulates the aggregation and toxicity of expanded pol...
Saved in:
| Main Authors: | Kate M Van Pelt, Matthias C Truttmann |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2025-06-01
|
| Series: | PLoS Genetics |
| Online Access: | https://doi.org/10.1371/journal.pgen.1011723 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Pre-clinical model of dysregulated FicD AMPylation causes diabetes by disrupting pancreatic endocrine homeostasis
by: Amanda K. Casey, et al.
Published: (2025-05-01) -
An interdomain sector mediating allostery in Hsp70 molecular chaperones
by: Robert G Smock, et al.
Published: (2010-09-01) -
Infancy‐onset diabetes caused by de‐regulated AMPylation of the human endoplasmic reticulum chaperone BiP
by: Luke A Perera, et al.
Published: (2023-01-01) -
Hsp70: A Multifunctional Chaperone in Maintaining Proteostasis and Its Implications in Human Disease
by: Manish Kumar Singh, et al.
Published: (2025-03-01) -
The chaperone BAG6 captures dislocated glycoproteins in the cytosol.
by: Jasper H L Claessen, et al.
Published: (2014-01-01)