Matches in SemOpenAlex for { <https://semopenalex.org/work/W3016687527> ?p ?o ?g. }
Showing items 1 to 60 of
60
with 100 items per page.
- W3016687527 endingPage "1" @default.
- W3016687527 startingPage "1" @default.
- W3016687527 abstract "Living proteomes are necessarily far from equilibrium. Otherwise cells could not use the energy released by phase separation to organize protein activities in space and time. It is paradoxical, then, that reducing protein influx into the proteome -- which should promote equilibration -- instead prolongs the lives of organisms from yeast to human. We therefore reasoned that kinetic barriers must exist to delay equilibration, and that these decrease with protein influx. We further hypothesized that the probabilistic nucleation of protein self-assemblies -- or deposits -- could underlie those barriers. To investigate the effects of influx on protein deposition, we probed phase boundaries and nucleation barriers for structurally diverse protein assemblies at different rates of translation initiation in living cells. We discovered that at protein concentrations that were globally supersaturated with respect to deposition as amyloids or other ordered phases, rapid translation promoted nucleation and thereby equilibration of that protein. We tentatively attribute this effect to unexpectedly slow diffusion of proteins away from sites of translation. The resulting local accumulation appears to facilitate protein clustering into nucleation competent multimers, even at global concentrations that are subsaturated with respect to liquid-liquid phase separation. Finally, we show that longevity-enhancing reductions in global protein initiation, as occur during stress responses or calorie restriction, similarly sharpen phase boundaries and nucleation barriers. Together, these observations suggest that living proteomes are supersaturated with respect to highly ordered, collectively lethal deposits. Support or Funding Information This work was funded by NIH Director’s Early Independence Award DP5-OD009152, NIH grant P30 AG035982, and the Stowers Institute for Medical Research." @default.
- W3016687527 created "2020-04-24" @default.
- W3016687527 creator A5057607550 @default.
- W3016687527 creator A5058446312 @default.
- W3016687527 creator A5071548048 @default.
- W3016687527 date "2020-04-01" @default.
- W3016687527 modified "2023-10-14" @default.
- W3016687527 title "Translation Initiation Rates Govern Protein Self‐Assembly In Vivo" @default.
- W3016687527 doi "https://doi.org/10.1096/fasebj.2020.34.s1.07306" @default.
- W3016687527 hasPublicationYear "2020" @default.
- W3016687527 type Work @default.
- W3016687527 sameAs 3016687527 @default.
- W3016687527 citedByCount "0" @default.
- W3016687527 crossrefType "journal-article" @default.
- W3016687527 hasAuthorship W3016687527A5057607550 @default.
- W3016687527 hasAuthorship W3016687527A5058446312 @default.
- W3016687527 hasAuthorship W3016687527A5071548048 @default.
- W3016687527 hasConcept C104317684 @default.
- W3016687527 hasConcept C105580179 @default.
- W3016687527 hasConcept C12554922 @default.
- W3016687527 hasConcept C149364088 @default.
- W3016687527 hasConcept C185592680 @default.
- W3016687527 hasConcept C207001950 @default.
- W3016687527 hasConcept C54355233 @default.
- W3016687527 hasConcept C55493867 @default.
- W3016687527 hasConcept C70721500 @default.
- W3016687527 hasConcept C86803240 @default.
- W3016687527 hasConcept C95444343 @default.
- W3016687527 hasConceptScore W3016687527C104317684 @default.
- W3016687527 hasConceptScore W3016687527C105580179 @default.
- W3016687527 hasConceptScore W3016687527C12554922 @default.
- W3016687527 hasConceptScore W3016687527C149364088 @default.
- W3016687527 hasConceptScore W3016687527C185592680 @default.
- W3016687527 hasConceptScore W3016687527C207001950 @default.
- W3016687527 hasConceptScore W3016687527C54355233 @default.
- W3016687527 hasConceptScore W3016687527C55493867 @default.
- W3016687527 hasConceptScore W3016687527C70721500 @default.
- W3016687527 hasConceptScore W3016687527C86803240 @default.
- W3016687527 hasConceptScore W3016687527C95444343 @default.
- W3016687527 hasIssue "S1" @default.
- W3016687527 hasLocation W30166875271 @default.
- W3016687527 hasOpenAccess W3016687527 @default.
- W3016687527 hasPrimaryLocation W30166875271 @default.
- W3016687527 hasRelatedWork W1593482576 @default.
- W3016687527 hasRelatedWork W1993437765 @default.
- W3016687527 hasRelatedWork W2036533527 @default.
- W3016687527 hasRelatedWork W2123853558 @default.
- W3016687527 hasRelatedWork W2198850752 @default.
- W3016687527 hasRelatedWork W2519825823 @default.
- W3016687527 hasRelatedWork W2622510373 @default.
- W3016687527 hasRelatedWork W2764188251 @default.
- W3016687527 hasRelatedWork W4224218201 @default.
- W3016687527 hasRelatedWork W4243472649 @default.
- W3016687527 hasVolume "34" @default.
- W3016687527 isParatext "false" @default.
- W3016687527 isRetracted "false" @default.
- W3016687527 magId "3016687527" @default.
- W3016687527 workType "article" @default.