Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease
Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease
Neurodegenerative diseases and other proteinopathies constitute a class of several dozen illnesses etiologically linked to pathological protein misfolding and aggregation. Because of this strong association with disease pathology, cell death, and aging, accumulation of proteins in aggregates or aggregation-associated structures (inclusions) has come to be regarded by many as a deleterious process, to be avoided if possible. Recent work has led us to see inclusion structures and disordered aggregate-like protein mixtures (which we call dynamic droplets) in a new light: not necessarily as a result of a pathological breakdown of cellular order, but as an elaborate cellular architecture regulating function and stress response. In this review, we discuss what is currently known about the role of inclusion structures in cellular homeostasis, stress response, toxicity, and disease. We will focus on possible mechanisms of aggregate toxicity, in contrast to the homeostatic function of several inclusion structures.
Aging/physiology, Animals, Homeostasis/physiology, Humans, Inclusion Bodies/pathology, Models, Biological, Protein Aggregates/physiology, Proteostasis Deficiencies/physiopathology, Stress, Physiological/physiology
401-415
Amen, Triana
388dc540-e819-4d07-8f1e-ee0f3949a54b
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f
1 February 2015
Amen, Triana
388dc540-e819-4d07-8f1e-ee0f3949a54b
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f
Amen, Triana and Kaganovich, Daniel
(2015)
Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease.
Cellular and Molecular Life Sciences, 72 (3), .
(doi:10.1007/s00018-014-1740-y).
Abstract
Neurodegenerative diseases and other proteinopathies constitute a class of several dozen illnesses etiologically linked to pathological protein misfolding and aggregation. Because of this strong association with disease pathology, cell death, and aging, accumulation of proteins in aggregates or aggregation-associated structures (inclusions) has come to be regarded by many as a deleterious process, to be avoided if possible. Recent work has led us to see inclusion structures and disordered aggregate-like protein mixtures (which we call dynamic droplets) in a new light: not necessarily as a result of a pathological breakdown of cellular order, but as an elaborate cellular architecture regulating function and stress response. In this review, we discuss what is currently known about the role of inclusion structures in cellular homeostasis, stress response, toxicity, and disease. We will focus on possible mechanisms of aggregate toxicity, in contrast to the homeostatic function of several inclusion structures.
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Published date: 1 February 2015
Keywords:
Aging/physiology, Animals, Homeostasis/physiology, Humans, Inclusion Bodies/pathology, Models, Biological, Protein Aggregates/physiology, Proteostasis Deficiencies/physiopathology, Stress, Physiological/physiology
Identifiers
Local EPrints ID: 475690
URI: http://eprints.soton.ac.uk/id/eprint/475690
ISSN: 1420-682X
PURE UUID: 79a9a516-2b67-4d3a-83b2-e87599312174
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Date deposited: 24 Mar 2023 17:56
Last modified: 17 Mar 2024 04:22
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Author:
Triana Amen
Author:
Daniel Kaganovich
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