Molecular Determinants of Protein Assemblies in Health and Disease

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Background

Proteins/peptides can self-assemble to form supramolecular entities called “aggregates”. Protein aggregation is a phenomenon that can be both directed and inadvertent; the latter is often proceeded by proteotoxic insults wherein proteins self-associate to form higher-order structures implicated in disease. Conversely, certain proteins have evolved to self-assemble to perform beneficial roles in the organism. Accumulating evidence highlights protein self-assembly into either dense liquid-like compartments or solid-like agglomerates in physiological settings. Depending on the fate of the resulting structures, these could participate in different cellular functions. While aberrant phase transitions that lead to irreversible, solid-like aggregates (e.g., amyloid fibrils) are signatures of degenerative diseases, a regulated biomolecular assembly such as in cytoskeletal filaments, plays a functional role in the cell. Moreover, crosstalk between proteins and nucleic acids has been indicated to generate co-assembled local clusters, which “form and dissolve” in response to external cues linked with diverse processes including stress response, DNA repair, and gene regulation.

Biomolecular assemblies can span several structural and material phases. Proteins can switch between soluble and aggregated states in response to subtle changes in intrinsic (post-translational modifications, mutations) and extrinsic factors (pH, temperature, salt concentration). Further, phase-separated proteins can often progressively transition to more irreversible aggregated states such as the amyloid-like state, a phenomenon expedited by mutations and other factors. Given that protein function typically hinges on the ability to interact with other proteins or form higher-order structures, proteostasis mechanisms must ensure tight regulation of their assembly and disassembly. Identifying the molecular driving forces for biomolecular assembly is, therefore, crucial to understand how living systems deal with this delicate balance between function and disease. In this edition, we aim to feature findings that highlight different aspects of biomolecular self-assembly in health and in sickness, including active mechanisms regulating protein assembly in living systems.

This Research Topic aims to shed light on functional aspects of supramolecular protein structures and biomolecular condensates, addressing their role in various biological functions as well as in the pathophysiology of diseases. We invite Original Research, Review, Mini-Review, Perspective, Hypothesis and Theory, Case reports, and Opinion articles including, but not limited to the following themes:

● Role of phase separation in physiological and pathophysiological aggregation

● Spatiotemporal control of intracellular phase transitions and aggregation behavior

● Factors influencing the formation and dissociation of “functional protein assemblies” such as condensates, membrane-less organelles, and functional amyloids

● Post-translational modifications and their role in regulating biological assemblies

● Pathophysiology of proteinopathies

● Structural diversity of protein aggregates

● Mechanistic aspects of model disordered proteins

● Influence of oxidative stress in protein assembly

● Model organisms to study protein assemblies

● Design of functional synthetic protein assemblies



Prof. Salvador Ventura Zamora holds patents related to this Research Topic, all other Topic Editors declare no conflict of interest

Keywords: Protein homeostasis; Protein aggregates; Phase separation; Protein condensates; Amyloids; Proteotoxicity

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Participating Journals

  • Frontiers in Chemistry

    • Protein Biochemistry for Basic and Applied SciencesOffline

    • 3.8 impact factor
    • 8.5 citescore

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