Stress‐induced mRNP granules: Form and function of processing bodies and stress granules

Advanced Review

Anna R. Guzikowski, Yang S. Chen, Brian M. Zid

Published Online: Feb 21 2019

DOI: 10.1002/wrna.1524

Full article on Wiley Online Library: HTML PDF

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In response to stress, cells must quickly reprogram gene expression to adapt and survive. This is achieved in part by altering levels of mRNAs and their translation into proteins. Recently, the formation of two stress‐induced messenger ribonucleoprotein (mRNP) assemblies named stress granules and processing bodies has been postulated to directly impact gene expression during stress. These assemblies sequester and concentrate specific proteins and RNAs away from the larger cytoplasm during stress, thereby providing a layer of posttranscriptional gene regulation with the potential to directly impact mRNA levels, protein translation, and cell survival. The function of these granules has generally been ascribed either by the protein components concentrated into them or, more broadly, by global changes that occur during stress. Recent proteome‐ and transcriptome‐wide studies have provided a more complete view of stress‐induced mRNP granule composition in varied cell types and stress conditions. However, direct measurements of the phenotypic and functional consequences of stress granule and processing body formation are lacking. This leaves our understanding of their roles during stress incomplete. Continued study into the function of these granules will be an important part in elucidating how cells respond to and survive stressful environmental changes. This article is categorized under: Translation > Translation Regulation RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes RNA Export and Localization > RNA Localization

Interactions between mammalian PB and SG protein components. Gene names of proteins with more than 15 interacting protein components in PBs are shown (left network) while those with more than 30 interacting protein components in SGs are shown (right network). Proteins that were identified as essential components for PB or SG assembly are highlighted in red; these tend to have increased numbers of interacting partners. Mammalian interactome datasets of PB and SG components are from Youn et al. (). The mammalian SG proteome is from S. Jain et al. () and the PB proteome is from Hubstenberger et al. ()

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Model for composition dynamics and potential function of stress‐induced mRNP granules. Lines with double arrows show that mRNAs associated with RBPs move in and out of stress‐induced mRNP granules. Dashed lines with inhibitory arrows show that mRNAs engaged in translation are excluded from stress‐induced mRNP granules

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Diverse sets of interactions drive mRNP granule assembly and LLPS. Five classes of interactions that contribute to SG and PB formation are modeled. Different protein–protein, protein–RNA, and RNA–RNA interactions contribute to phase separation and drive the formation of stress‐induced mRNP granules

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