Journal article
Protein Aggregation and Disaggregation in Cells and Development
Journal of molecular biology, Vol.433(21), pp.167215-167215
10/15/2021
DOI: 10.1016/j.jmb.2021.167215
PMCID: PMC8530975
PMID: 34450138
Abstract
[Display omitted]
•Regulated aggregation affects protein storage, activity and spatial distribution.•Many “bodies” historically connected to cell and development are protein condensates.•Physiological aggregates are regulated, reversible, and often multifunctional.•Chaperones, protein modification, local milieu and co-aggregates alter aggregation.•Exploring multiple experimental systems helps identify regulators of aggregation.
Protein aggregation is a feature of numerous neurodegenerative diseases. However, regulated, often reversible, formation of protein aggregates, also known as condensates, helps control a wide range of cellular activities including stress response, gene expression, memory, cell development and differentiation. This review presents examples of aggregates found in biological systems, how they are used, and cellular strategies that control aggregation and disaggregation. We include features of the aggregating proteins themselves, environmental factors, co-aggregates, post-translational modifications and well-known aggregation-directed activities that influence their formation, material state, stability and dissolution. We highlight the emerging roles of biomolecular condensates in early animal development, and disaggregation processing proteins that have recently been shown to play key roles in gametogenesis and embryogenesis.
Details
- Title: Subtitle
- Protein Aggregation and Disaggregation in Cells and Development
- Creators
- Jan S Fassler - Department of Biology, University of Iowa, Iowa City, IA 52242, United StatesSydney Skuodas - Department of Biology, University of Iowa, Iowa City, IA 52242, United StatesDaniel L Weeks - Department of Biochemistry, University of Iowa, Iowa City, IA 52242, United StatesBryan T Phillips - Department of Biology, University of Iowa, Iowa City, IA 52242, United States
- Resource Type
- Journal article
- Publication Details
- Journal of molecular biology, Vol.433(21), pp.167215-167215
- DOI
- 10.1016/j.jmb.2021.167215
- PMID
- 34450138
- PMCID
- PMC8530975
- NLM abbreviation
- J Mol Biol
- ISSN
- 0022-2836
- eISSN
- 1089-8638
- Publisher
- Elsevier Ltd
- Language
- English
- Date published
- 10/15/2021
- Academic Unit
- Stead Family Department of Pediatrics; Biology; Biochemistry and Molecular Biology
- Record Identifier
- 9984217537402771
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