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A particular type of physiological condensate called stress granules (SGs) has gained increasing interest due to its role in the cellular stress response and various diseases. SGs, composed of several hundred RNA\u2010binding proteins, form transiently in response to stress to protect mRNAs from translation and disassemble when the stress subsides. Interestingly, SGs contain several aggregation\u2010prone proteins, such as TDP\u201043, FUS, hnRNPA1, and others, which are typically found in pathological inclusions seen in autopsy tissues from amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) patients. Moreover, mutations in these genes lead to the familial form of ALS and FTD. This has led researchers to propose that pathological aggregation is seeded by aberrant SGs: SGs that fail to properly disassemble, lose their dynamic properties, and become pathological condensates which finally \u2018mature\u2019 into aggregates. Here, we discuss the evidence supporting this model for various ALS\/FTD\u2010associated proteins. We further continue to focus on molecular chaperone\u2010mediated regulation of ALS\/FTD\u2010associated physiological condensates on one hand, and pathological condensates on the other. In addition to SGs, we review ALS\/FTD\u2010relevant nuclear condensates, namely paraspeckles, anisosomes, and nucleolar amyloid bodies, and discuss their emerging regulation by chaperones. As the majority of chaperoning mechanisms regulate physiological condensate disassembly, we highlight parallel themes of physiological and pathological condensation regulation across different chaperone families, underscoring the potential for early disease intervention.<\/jats:p>","DOI":"10.1111\/febs.17390","type":"journal-article","created":{"date-parts":[[2025,1,5]],"date-time":"2025-01-05T12:04:25Z","timestamp":1736078665000},"page":"3271-3297","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Regulation of physiological and pathological condensates by molecular chaperones"],"prefix":"10.1111","volume":"292","author":[{"given":"Nadeen","family":"Akaree","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Rappaport Faculty of Medicine Technion\u2010Israel Institute of Technology  Haifa 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