Proteins are known to form multi-molecular complexes to execute diverse functions. Research in recent years has led to the identification of a variety of higher-ordered protein assemblies (e.g. aggregates, aggresomes, inclusions, stress foci and stress granules, CytoQ, IMiQ, IPOD, and JUNQ/INQ) that are closely associated with cellular changes in aging and in common neurodegenerative diseases such as Alzheimer’s Disease (AD), Parkinson’s Disease (PD), amyotrophic lateral sclerosis (ALS), and Huntington’s Disease (HD). Moreover, the latest discovery of intracellular protein phase separation suggests that the formation of protein assemblies is a well-regulated process associated with functional switches. Therefore, understanding the functional roles of these protein assemblies, as well as the molecular events underlying their synthesis, formation, conversion, recognition, dissociation, and degradation will promote fundamental understanding of the mechanisms of aging with potential relevance for neurodegenerative disorders.
In this Research Topic, we aim to gather original research (research articles and reports), mini-review and review articles, and methodological approaches on the synthesis, formation, conversion and regulation of protein assemblies in aging and age-related diseases. Specific topics can include but are not limited to:
- Age-associated protein assemblies and their physiological roles;
- Molecular mechanisms of protein assembly formation, dissociation, and degradation;
- Epigenetic alterations affecting proteostasis pathways in aging;
- Protein assemblies and proteomic analysis in neurodegenerative diseases;
- Protein phase separation in protein aggregation and disaggregation;
- Models of protein assembly-associated age-related diseases;
- Potential drug targets and approaches for protein assembly-associated age-related diseases.
Proteins are known to form multi-molecular complexes to execute diverse functions. Research in recent years has led to the identification of a variety of higher-ordered protein assemblies (e.g. aggregates, aggresomes, inclusions, stress foci and stress granules, CytoQ, IMiQ, IPOD, and JUNQ/INQ) that are closely associated with cellular changes in aging and in common neurodegenerative diseases such as Alzheimer’s Disease (AD), Parkinson’s Disease (PD), amyotrophic lateral sclerosis (ALS), and Huntington’s Disease (HD). Moreover, the latest discovery of intracellular protein phase separation suggests that the formation of protein assemblies is a well-regulated process associated with functional switches. Therefore, understanding the functional roles of these protein assemblies, as well as the molecular events underlying their synthesis, formation, conversion, recognition, dissociation, and degradation will promote fundamental understanding of the mechanisms of aging with potential relevance for neurodegenerative disorders.
In this Research Topic, we aim to gather original research (research articles and reports), mini-review and review articles, and methodological approaches on the synthesis, formation, conversion and regulation of protein assemblies in aging and age-related diseases. Specific topics can include but are not limited to:
- Age-associated protein assemblies and their physiological roles;
- Molecular mechanisms of protein assembly formation, dissociation, and degradation;
- Epigenetic alterations affecting proteostasis pathways in aging;
- Protein assemblies and proteomic analysis in neurodegenerative diseases;
- Protein phase separation in protein aggregation and disaggregation;
- Models of protein assembly-associated age-related diseases;
- Potential drug targets and approaches for protein assembly-associated age-related diseases.
