Stressed cells don't destroy. They condense — sequestering vulnerable proteins into chaperone-tended droplets that preserve their cargo until the storm passes.
That is adaptation. Reversible. Liquid. Kept alive by chaperones. Not the old degradation paradigm, but a cell that holds its proteome in trust.
Each division spends a little of this capacity. Aggregates partition to the mother; the daughter starts fresh. By the time an old mother meets the next perturbation, the response that defines her has been exhausted — by the act of living.
A cartoon of the preservation response — and what becomes of it across the replicative lifespan.
Heat shock. Chaperones rush to the nucleolus and cytosolic foci. The cytoplasm folds itself into reversible condensates that hold their cargo in trust.
This is what adaptation looks like. And this is what fades with age.
From Ali et al., Nature Cell Biology (2023) · Supplementary Movie 3
Condensation is adaptation. Chaperones keep it alive. Ageing wears it down.
Stressed cells don't disassemble — they hold. Orphan ribosomal proteins, translation factors, vulnerable cargo of every kind: gathered into chaperone-tended droplets, kept reversible until the perturbation passes.
We map how the cell chooses what to keep — and how it lets it go.
Condensates are not deposits — they are stirred. Chaperones keep them liquid, reversible, addressable. The cargo is preserved precisely because it never settles.
We track this caretaking molecule by molecule — and the moment it fails. The line between preserved and aggregated is the line we want to draw.
The mother keeps what the daughter does not. Division after division, condensed and aggregated material is retained — and the same machinery that mounts the acute response is the machinery that holds the legacy.
Every division spends a little. By the last, there is nothing left to spend. We watch this drawdown in single cells — looking for what runs out first.
A stem cell is its responsiveness. When that response narrows, identity itself starts to age.
We are taking the question across kingdoms: does condensation-based capacity, exhausted, explain the loss of regenerative power?
Trained in biochemistry at Bose Institute, University of Calcutta. Postdoctoral scholar in David Pincus's lab at the University of Chicago, where his work on the spatiotemporal regulation of the heat shock response — including the discovery of chaperone-stirred condensates that protect orphan ribosomal proteins (Nature Cell Biology, 2023, cover feature) — laid the foundation for the lab's central question.
PhD positions for students with backgrounds in molecular biology, genetics, biochemistry, or quantitative imaging.
Reagents, yeast strain library, microscopy stewardship, and the everyday infrastructure of doing rigorous experiments.
Cells respond to proteotoxic stress by sequestering orphan ribosomal proteins into chaperone-stirred condensates that preserve, rather than degrade, their cargo — a striking instance of dynamic adaptation at the heart of proteostasis.
Full publication list on ORCID →
A new lab. Recruiting. We run weekly data clubs on raw data, not polished figures — because that's where the real conversation lives.
If our questions are yours — especially if you arrive from a different angle (biophysics, computation, evolution, medicine) — write to us.