Cancer and neurodegenerative diseases such as ALS often begin with subtle breakdowns inside cells.
Scientists have long searched for ways to intervene earlier, by targeting the internal systems that regulate growth and clear toxic proteins.
According to researchers at Scripps Research, a newly identified cellular structure could offer exactly that opportunity.
The team reported in Nature Structural and Molecular Biology on February 2, 2026, that certain biomolecular condensates inside cells are supported by a microscopic scaffold of protein filaments.
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The discovery suggests these structures, once considered too disordered to target with drugs, may in fact have defined architecture that can be manipulated.
From liquids to structure
Biomolecular condensates have been a major focus of cell biology over the past decade, particularly in research on phase separation, a process in which molecules cluster together much like oil separating from water.
First recognized as a widespread organizing principle in cells in the 2010s, these droplets were believed to behave like simple liquids without internal structure.
According to the Scripps team, that view is incomplete. Using cryo-electron tomography, the researchers examined a bacterial protein called PopZ and found that it assembles into thin filaments that weave together into a supportive network. The team reported that this scaffold determines the droplet’s physical properties.
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When the researchers engineered a mutant version of PopZ that could not form filaments, cells failed to grow properly and struggled to divide their DNA.
Why it matters
Although the experiments were conducted in bacteria, similar condensates in human cells help regulate cell division and remove damaged proteins.
Disruption of these processes has been linked to cancers and neurodegenerative disorders, including ALS.
By identifying a structural framework within condensates, the researchers suggest that future therapies could be designed to stabilize or modify these internal networks rather than targeting individual molecules alone.
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Sources: ScienceDaily and Nature
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