ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion through Increased Interactions with Endoplasmic Reticulum Proteostasis Factors

ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion through Increased Interactions with Endoplasmic Reticulum Proteostasis Factors

The extracellular aggregation of destabilized transthyretin (TTR) variants is implicated in the onset and pathogenesis of familial TTR-related amyloid diseases. One strategy to reduce the toxic, extracellular aggregation of TTR is to decrease the population of aggregation-prone proteins secreted fro...

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Bibliographic Details
Main Authors: Jaleh S. Mesgarzadeh, Isabelle C. Romine, Ethan M. Smith-Cohen, Julia M. D. Grandjean, Jeffery W. Kelly, Joseph C. Genereux, R. Luke Wiseman
Format: Article
Language:English
Published: MDPI AG 2022-05-01
Series:Cells
Subjects:
ER proteostasis
protein aggregation
amyloid disease
unfolded protein response (UPR)
ATF6
protein disulfide isomerase (PDI)
Online Access:https://www.mdpi.com/2073-4409/11/10/1661

Internet

https://www.mdpi.com/2073-4409/11/10/1661

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