» Articles » PMID: 22147700

Macromolecular Crowding Regulates Assembly of MRNA Stress Granules After Osmotic Stress: New Role for Compatible Osmolytes

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2011 Dec 8
PMID 22147700
Citations 43
Authors
Affiliations
Soon will be listed here.
Abstract

The massive uptake of compatible osmolytes such as betaine, taurine, and myo-inositol is a protective response shared by all eukaryotes exposed to hypertonic stress. Their accumulation results mostly from the expression of specific transporters triggered by the transcriptional factor NFAT5/TonEBP. This allows the recovery of the cell volume without increasing intracellular ionic strength. In this study we consider the assembly and dissociation of mRNA stress granules (SGs) in hypertonic-stressed cells and the role of compatible osmolytes. In agreement with in vitro results obtained on isolated mRNAs, both macromolecular crowding and a high ionic strength favor the assembly of SGs in normal rat kidney epithelial cells. However, after hours of constant hypertonicity, the slow accumulation in the cytoplasm of compatible osmolytes via specific transporters both reduces macromolecular crowding and ionic strength, thus leading to the progressive dissociation of SGs. In line with this, when cells are exposed to hypertonicity to accumulate a large amount of compatible osmolytes, the formation of SGs is severely impaired, and cells increase their chances of survival to another hypertonic episode. Altogether, these results indicate that the impact of compatible osmolytes on the mRNA-associated machineries and especially that associated with SGs may play an important role in cell resistance and adaption to hyperosmolarity in many tissues like kidney and liver.

Citing Articles

Dynamic composition of stress granules in Trypanosoma brucei.

Aye H, Li F, He C PLoS Pathog. 2024; 20(10):e1012666.

PMID: 39480887 PMC: 11556693. DOI: 10.1371/journal.ppat.1012666.


Cell stress and phase separation stabilize the monomeric state of pseudoisocyanine chloride employed as a self-assembly crowding sensor.

Pollak R, Koch L, Konig B, Ribeiro S, Samanta N, Huber K Commun Chem. 2024; 7(1):230.

PMID: 39375435 PMC: 11458801. DOI: 10.1038/s42004-024-01315-y.


Exploring the role of macromolecular crowding and TNFR1 in cell volume control.

Biswas P, Roy P, Jana S, Ray D, Das J, Chaudhuri B Elife. 2024; 13.

PMID: 39297502 PMC: 11581439. DOI: 10.7554/eLife.92719.


The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact.

van den Noort M, Drougkas P, Paulino C, Poolman B Elife. 2024; 12.

PMID: 38695350 PMC: 11065425. DOI: 10.7554/eLife.90996.


Interplay Between Intracellular Transport Dynamics and Liquid‒Liquid Phase Separation.

Zhang M, Zhang Z, Niu X, Ti H, Zhou Y, Gao B Adv Sci (Weinh). 2024; 11(19):e2308338.

PMID: 38447188 PMC: 11109639. DOI: 10.1002/advs.202308338.


References
1.
Minton A . Influence of excluded volume upon macromolecular structure and associations in 'crowded' media. Curr Opin Biotechnol. 1997; 8(1):65-9. DOI: 10.1016/s0958-1669(97)80159-0. View

2.
Pastre D, Hamon L, Mechulam A, Sorel I, Baconnais S, Curmi P . Atomic force microscopy imaging of DNA under macromolecular crowding conditions. Biomacromolecules. 2007; 8(12):3712-7. DOI: 10.1021/bm700856u. View

3.
Navarro P, Chiong M, Volkwein K, Moraga F, Ocaranza M, Jalil J . Osmotically-induced genes are controlled by the transcription factor TonEBP in cultured cardiomyocytes. Biochem Biophys Res Commun. 2008; 372(2):326-30. PMC: 2522383. DOI: 10.1016/j.bbrc.2008.05.067. View

4.
Minton A . Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol. 2000; 10(1):34-9. DOI: 10.1016/s0959-440x(99)00045-7. View

5.
Marenduzzo D, Finan K, Cook P . The depletion attraction: an underappreciated force driving cellular organization. J Cell Biol. 2006; 175(5):681-6. PMC: 2064666. DOI: 10.1083/jcb.200609066. View