Literature DB >> 28342303

Cell adaptation upon stress: the emerging role of membrane-less compartments.

Catherine Rabouille1, Simon Alberti2.   

Abstract

Cells under stress transition from a growth to a quiescent state. The conventional thinking is that this is achieved through transcriptional programs, translational regulation, protein degradation, and post-translational modifications. However, there is an increasing realization that stress adaptation also goes along with dramatic changes in the architecture and organization of cells. In particular, it seems to involve the formation of membrane-less compartments and macromolecular assemblies. We propose that cells make widespread use of this ability to change macromolecular organization to adapt to stress conditions and protect themselves. Here, we address what triggers the formation of these assemblies under stress conditions. We present examples illustrating that in some cases, sophisticated signaling pathways transmit environmental fluctuations from the outside to the inside and in others, that external fluctuations directly affect the internal conditions in cells. We further argue that changes in the organization of the cytoplasm and the formation of membrane-less compartments have many advantages over other ways of altering protein function, such as protein degradation, translation or transcription. Furthermore, membrane-less compartments may act as protective devices for key cellular components.
Copyright © 2017 Elsevier Ltd. All rights reserved.

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Year:  2017        PMID: 28342303     DOI: 10.1016/j.ceb.2017.02.006

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  28 in total

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Authors:  Daniel B Roche; Etienne Villain; Andrey V Kajava
Journal:  Protein Sci       Date:  2017-07-15       Impact factor: 6.725

2.  Weak protein-protein interactions in live cells are quantified by cell-volume modulation.

Authors:  Shahar Sukenik; Pin Ren; Martin Gruebele
Journal:  Proc Natl Acad Sci U S A       Date:  2017-06-12       Impact factor: 11.205

3.  Insights into the Role of P-Bodies and Stress Granules in Protein Quality Control.

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Journal:  Genetics       Date:  2019-07-08       Impact factor: 4.562

Review 4.  Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior.

Authors:  Titus M Franzmann; Simon Alberti
Journal:  J Biol Chem       Date:  2018-06-19       Impact factor: 5.157

5.  Membraneless Compartmentalization Facilitates Enzymatic Cascade Reactions and Reduces Substrate Inhibition.

Authors:  Taisuke Kojima; Shuichi Takayama
Journal:  ACS Appl Mater Interfaces       Date:  2018-09-14       Impact factor: 9.229

6.  Monitoring and Quantification of the Dynamics of Stress Granule Components in Living Cells by Fluorescence Decay After Photoactivation.

Authors:  Anna-Carina Söhnel; Nataliya I Trushina; Roland Brandt
Journal:  Methods Mol Biol       Date:  2022

7.  Tuning C-Phycocyanin Photoactivity via pH-Mediated Assembly-Disassembly.

Authors:  Ying Li; Richard Gillilan; Alireza Abbaspourrad
Journal:  Biomacromolecules       Date:  2021-11-12       Impact factor: 6.978

Review 8.  Mutations, protein homeostasis, and epigenetic control of genome integrity.

Authors:  Jinglin Lucy Xie; Daniel F Jarosz
Journal:  DNA Repair (Amst)       Date:  2018-08-23

Review 9.  Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans.

Authors:  Gea Cereghetti; Shady Saad; Reinhard Dechant; Matthias Peter
Journal:  Cell Cycle       Date:  2018-08-02       Impact factor: 4.534

Review 10.  Why Do Disordered and Structured Proteins Behave Differently in Phase Separation?

Authors:  Huan-Xiang Zhou; Valery Nguemaha; Konstantinos Mazarakos; Sanbo Qin
Journal:  Trends Biochem Sci       Date:  2018-04-30       Impact factor: 13.807

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