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Protein aggregation as a mechanism of adaptive cellular responses


Coalescence of proteins into different types of intracellular bodies has surfaced as a widespread adaptive mechanism to re-organize cells and cellular functions in response to specific cues. These structures, composed of proteins or protein-mRNA-complexes, regulate cellular processes through modulating enzymatic activities, gene expression or shielding macromolecules from damage. Accordingly, such bodies are associated with a wide-range of processes, including meiosis, memory-encoding, host-pathogen interactions, cancer, stress responses, as well as protein quality control, DNA replication stress and aneuploidy. Importantly, these distinct coalescence responses are controlled, and in many cases regulated by chaperone proteins. While cells can tolerate and proficiently coordinate numerous distinct types of protein bodies, some of them are also intimately linked to diseases or the adverse effects of aging. Several protein bodies that differ in composition, packing, dynamics, size, and localization were originally discovered in budding yeast. Here, we provide a concise and comparative review of their nature and nomenclature.

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We apologize to colleagues whose work we were unable to cite due to length restrains. We are thankful to Fabrice Caudron, Marek Krzyzanowski and Asim Sengör for comments on the manuscript. JS acknowledges FEBS and the Finnish Cultural Foundation and YB the European Research council and the ETH Zurich for financial support.

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Correspondence to Juha Saarikangas or Yves Barral.

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Communicated by M. Kupiec.

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Saarikangas, J., Barral, Y. Protein aggregation as a mechanism of adaptive cellular responses. Curr Genet 62, 711–724 (2016).

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  • Compartmentalization
  • Mnemon
  • Adaptopod
  • Phase transition
  • Proteostasis
  • Amyloid