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dc.contributor.authorvan Tartwijk, Francesca
dc.contributor.authorKaminski, Clemens
dc.date.accessioned2022-05-26T23:30:31Z
dc.date.available2022-05-26T23:30:31Z
dc.identifier.issn2701-0198
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337521
dc.description.abstractThe 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.
dc.description.sponsorshipMedImmune, Infinitus (China) Ltd
dc.publisherWiley
dc.rightsAll Rights Reserved
dc.rights.urihttp://www.rioxx.net/licenses/all-rights-reserved
dc.subjectbiomolecular condensation
dc.subjectcytoplasmic self-organisation
dc.subjectlocal protein synthesis
dc.subjectmacromolecular crowding
dc.subjectmacromolecular interactions
dc.subjectribonucleoprotein granules
dc.subjectcytoplasmic properties
dc.subjectstress responses
dc.subjectextremophiles
dc.titleProtein Condensation, Cellular Organization, and Spatiotemporal Regulation of Cytoplasmic Properties
dc.typeArticle
dc.publisher.departmentDepartment of Chemical Engineering & Biotechnology
dc.date.updated2022-05-25T15:33:27Z
prism.publicationNameAdvanced Biology
dc.identifier.doi10.17863/CAM.84936
dcterms.dateAccepted2022-05-16
rioxxterms.versionofrecord10.1002/adbi.202101328
rioxxterms.versionAM
dc.contributor.orcidvan Tartwijk, Francesca [0000-0002-9795-2571]
dc.contributor.orcidKaminski, Clemens [0000-0002-5194-0962]
dc.identifier.eissn2701-0198
rioxxterms.typeJournal Article/Review
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/H018301/1)
pubs.funder-project-idMedical Research Council (MR/K015850/1)
pubs.funder-project-idMedical Research Council (MR/K02292X/1)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/L015889/1)
pubs.funder-project-idWellcome Trust (203249/Z/16/Z)
pubs.funder-project-idEngineering and Physical Sciences Research Council (1946113)
cam.issuedOnline2022-07-07
cam.orpheus.successMon Jul 11 08:50:17 BST 2022 - Embargo updated*
cam.orpheus.success2022/07/29
cam.orpheus.counter5
cam.depositDate2022-05-25
pubs.licence-identifierapollo-deposit-licence-2-1
pubs.licence-display-nameApollo Repository Deposit Licence Agreement
rioxxterms.freetoread.startdate2023-07-08


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