Stress-specific aggregation of proteins in the amyloid bodies.

Abstract:

:Physiological amyloid aggregation occurs within the nuclei of stress-treated cells. These structures, termed Amyloid bodies (A-bodies), assemble through the rapid accumulation of proteins into dense membrane-less organelles, which possess the same biophysical properties as plaques observed in many amyloid-based diseases. Here, we demonstrate that A-body proteomic compositions vary significantly between stimuli, as constituent proteins can be sequestered by one or more stressors. Stimulus exposure alone was insufficient to induce aggregation, demonstrating that this pathway is not regulated solely by stress-induced conformational changes of the A-body targets. We propose that different environmental conditions induce the formation of A-body subtypes containing distinct protein residents. This selective immobilization of proteins may have evolved as a finely tuned mechanism for surviving divergent stressors.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Marijan D,Tse R,Elliott K,Chandhok S,Luo M,Lacroix E,Audas TE

doi

10.1002/1873-3468.13597

subject

Has Abstract

pub_date

2019-11-01 00:00:00

pages

3162-3172

issue

22

eissn

0014-5793

issn

1873-3468

journal_volume

593

pub_type

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