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Anna Leder @annaleder.bsky.social · 21/09/2026

A huge thank you to my co-first authors Raju and @masgu.bsky.social, our collaborators Nadinath Nillegoda, @trumanlab.bsky.social, @paolodelosrios.bsky.social, @chercheurjuteux.com, @hillerlab.bsky.social and everyone else involved!

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Anna Leder @annaleder.bsky.social · 21/09/2026

🧬 Happy to see our paper finally out! Here we show that a post-translational modification tunes Hsp70–J-domain protein interaction by unfolding of the J-domain. This either blocks Hsp70 engagement or leads to protein degradation. Check out how this phospho-switch rewires chaperone networks:

nature.com

A conserved tyrosine motif encodes a structural vulnerability controlling stability and activity across J-domain proteins - Communications Biology

NMR spectroscopy and functional assays define a conserved tyrosine motif outside the canonical J-domain core of J-domain proteins. The motif stabilizes the fold, and its phosphomimetic perturbation dr...

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Anna Leder @annaleder.bsky.social · 11/08/2025

Great teamwork with @masgu.bsky.social and I am very thankful for the huge support by Sebastian @hillerlab.bsky.social and Anne @spanglab.bsky.social!

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Anna Leder @annaleder.bsky.social · 11/08/2025

PDIA6 forms the scaffold of these phase separated condensates and we resolve the underlying calcium-dependent mechanism. Further chaperones - including Hsp70, Hsp40 and Hsp90 - are recruited into the condensates, where they enhance client proteins folding, functioning as “folding factories”.

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Anna Leder @annaleder.bsky.social · 11/08/2025

Happy to share my first publication, where we present our discovery of multi-chaperone condensates that orchestrate protein folding in the endoplasmic reticulum! www.nature.com/articles/s41...

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Anna Leder @annaleder.bsky.social · 02/06/2025

Check out this amazing work on the functional cycle of Hsp70 BiP NBD at atomic resolution by @masgu.bsky.social

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