A well-functioning proteome is essential for the survival of cells, orchestrating critical processes like cell structure, development and signaling. The balance and dynamic regulation of proteins ensure their proper functionality. This equilibrium, known as protein homeostasis or proteostasis, involves maintaining proteins through proper synthesis, folding, trafficking, and degradation of proteins. However, it faces a myriad of challenges, including environmental stress, diseases, and aging. The loss of proteostasis can lead to major consequences at both cellular and physiological levels, such as the formation of protein aggregates and neurodegeneration. In essence, the maintenance of protein homeostasis is a critical aspect of life.
The proteostasis machinery, comprising molecular chaperones, the ubiquitin-proteasome system and other components, combats aberrant proteins and their emergence. While many contributors to a healthy proteome have been identified, the intriguing question persists: why do some misfolded proteins become cytotoxic while others do not? Unraveling this mystery is pivotal for comprehending the connections between protein homeostasis and the onset of diseases, particularly those encompassing neurodegeneration, and to advance the development of therapeutics countering them. Furthermore, delving into how healthy cells and organisms maintain their dynamic and adaptive proteome compared to their diseased counterparts is essential. Such comparative exploration provides valuable insights into the intricacies of proteostasis and its role in maintaining cellular health. In this research topic, we aim to collect submissions of pre-clinical research articles on protein homeostasis in the contexts of health, neurodegenerative disease and aging with a particular emphasis on neurodegeneration.
We encourage reports encompassing in vitro studies, cellular models and animals. We want to emphasize our interest in contributions describing novel approaches to explore this subject, such as newly developed reporter proteins to study neurodegeneration. Additionally, we seek articles employing less commonly used methodologies, underscoring their significance in the field. This may involve for example single-molecule tracking or mathematical modelling. We also welcome (mini) reviews that summarize recent methodologies and/or findings and discuss their implications.
· Molecular and cellular mechanisms of protein misfolding, aggregation and clearance of aberrant proteins and their roles in neurodegeneration, including traumatic brain injury.
· Contribution of stressors to protein misfolding and aggregation, e.g. environmental factors.
· Consequences of acute vs chronic protein homeostasis stress.
· Connections to other cellular homeostasis machineries, such as signal transduction processes.
Keywords:
molecular chaperones, protein aggregation, protein misfolding, neurodegeneration, aging, proteostasis
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
A well-functioning proteome is essential for the survival of cells, orchestrating critical processes like cell structure, development and signaling. The balance and dynamic regulation of proteins ensure their proper functionality. This equilibrium, known as protein homeostasis or proteostasis, involves maintaining proteins through proper synthesis, folding, trafficking, and degradation of proteins. However, it faces a myriad of challenges, including environmental stress, diseases, and aging. The loss of proteostasis can lead to major consequences at both cellular and physiological levels, such as the formation of protein aggregates and neurodegeneration. In essence, the maintenance of protein homeostasis is a critical aspect of life.
The proteostasis machinery, comprising molecular chaperones, the ubiquitin-proteasome system and other components, combats aberrant proteins and their emergence. While many contributors to a healthy proteome have been identified, the intriguing question persists: why do some misfolded proteins become cytotoxic while others do not? Unraveling this mystery is pivotal for comprehending the connections between protein homeostasis and the onset of diseases, particularly those encompassing neurodegeneration, and to advance the development of therapeutics countering them. Furthermore, delving into how healthy cells and organisms maintain their dynamic and adaptive proteome compared to their diseased counterparts is essential. Such comparative exploration provides valuable insights into the intricacies of proteostasis and its role in maintaining cellular health. In this research topic, we aim to collect submissions of pre-clinical research articles on protein homeostasis in the contexts of health, neurodegenerative disease and aging with a particular emphasis on neurodegeneration.
We encourage reports encompassing in vitro studies, cellular models and animals. We want to emphasize our interest in contributions describing novel approaches to explore this subject, such as newly developed reporter proteins to study neurodegeneration. Additionally, we seek articles employing less commonly used methodologies, underscoring their significance in the field. This may involve for example single-molecule tracking or mathematical modelling. We also welcome (mini) reviews that summarize recent methodologies and/or findings and discuss their implications.
· Molecular and cellular mechanisms of protein misfolding, aggregation and clearance of aberrant proteins and their roles in neurodegeneration, including traumatic brain injury.
· Contribution of stressors to protein misfolding and aggregation, e.g. environmental factors.
· Consequences of acute vs chronic protein homeostasis stress.
· Connections to other cellular homeostasis machineries, such as signal transduction processes.
Keywords:
molecular chaperones, protein aggregation, protein misfolding, neurodegeneration, aging, proteostasis
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.