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Translating the Chaperone Code

Molecular chaperones have been extensively studied for the last 50 years; they are highly conserved and are essential for many cellular processes.  Research has primarily focused on how chaperone function is regulated via transcription, expression of highly related paralogs and the suite of co-chaperone binding partners.


Despite this, we still know very little about the post-translational modification (PTM) of chaperone proteins and how these modifications may affect their cellular function.  Powerful technologies such as affinity purification of proteins coupled with tandem mass spectrometry (AP-MS/MS) have uncovered a substantial number of modified sites on both Hsp70 and Hsp90. These PTMs can be added and removed rapidly, allowing fine-tuning chaperone function when required. The large number of detected modifications such as phosphorylation, ubiquitination, SUMOylation and acetylation) suggest a “chaperone code” similar in nature to the combinatory PTM code that exists on histones.


We consider the chaperone code as the ultimate frontier in chaperone research. The understanding of the reciprocal interplay between chaperones and key signal transductions system will lead to an unprecedented ability to manipulate chaperone function for experimental and translational purposes. We conceived this symposium and related chaperone code club to unite like-minded researchers to collaborate in cracking this monumental biological conundrum.

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