title: Protein aggregation as a mechanism of adaptive cellular responses.
abstract: 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.
authors.affiliation: ETH Zurich, Institute of Biochemistry, Otto-Stern-Weg 3, 8093, Zurich, Switzerland. juha.saarikangas@bc.biol.ethz.ch.
authors.forename: Juha
authors.initials: J
authors.lastname: Saarikangas
authors.affiliation: ETH Zurich, Institute of Biochemistry, Otto-Stern-Weg 3, 8093, Zurich, Switzerland. yves.barral@bc.biol.ethz.ch.
authors.forename: Yves
authors.initials: Y
authors.lastname: Barral
mesh_terms: D000222:Adaptation, Physiological; D000375:Aging / Q000378:metabolism; D003594:Cytoplasmic Granules; D015870:Gene Expression; D006801:Humans; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D066329:Protein Aggregates; D066263:Protein Aggregation, Pathological / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D013312:Stress, Physiological; D015003:Yeasts / Q000235:genetics / Q000378:metabolism
chemical_list: D011328:Prions; D066329:Protein Aggregates; D011506:Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins
keywords: Adaptopod; Amyloid; Compartmentalization; Mnemon; Phase transition; Proteostasis