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Protein Condensation, Cellular Organization, and Spatiotemporal Regulation of Cytoplasmic Properties

Accepted version
Peer-reviewed

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Article

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Authors

van Tartwijk, Francesca  ORCID logo  https://orcid.org/0000-0002-9795-2571

Abstract

The cytoplasm is an aqueous, highly crowded solution of active macromolecules. Its properties influence the behavior of proteins, including their folding, their motion, and their interactions. In particular, proteins in the cytoplasm can interact to form phase- separated assemblies, so-called biomolecular condensates. The interplay between cytoplasmic properties and protein condensation is critical in a number of functional contexts and is the subject of this review. We first describe how cytoplasmic properties can affect protein behavior, in particular condensate formation. We then describe the functional implications of this interplay in three cellular contexts, which exemplify how protein self-organization can be adapted to support certain physiological phenotypes. First, we describe the formation of RNA-protein condensates in highly polarized cells such as neurons, where condensates play a critical role in the regulation of local protein synthesis. We then describe how different stressors trigger extensive reorganization of the cytoplasm, both through signaling pathways and through direct stress-induced changes in cytoplasmic properties. Finally, we describe changes in protein behavior and cytoplasmic properties that may occur in extremophiles, in particular organisms that have adapted to inhabit environments of extreme temperature, and discuss the implications and functional importance of these changes.

Description

Keywords

biomolecular condensation, cytoplasmic self-organisation, local protein synthesis, macromolecular crowding, macromolecular interactions, ribonucleoprotein granules, cytoplasmic properties, stress responses, extremophiles

Journal Title

Advanced Biology

Conference Name

Journal ISSN

2701-0198
2701-0198

Volume Title

Publisher

Wiley
Sponsorship
Engineering and Physical Sciences Research Council (EP/H018301/1)
Medical Research Council (MR/K015850/1)
Medical Research Council (MR/K02292X/1)
Engineering and Physical Sciences Research Council (EP/L015889/1)
Wellcome Trust (203249/Z/16/Z)
Engineering and Physical Sciences Research Council (1946113)
MedImmune, Infinitus (China) Ltd