Abstract

Decrypting the chaperone code

Highlights

  • Heat shock protein 90 (Hsp90) is a molecular chaperone involved in folding, stability, and activity of more than 300 proteins known as clients

  • Since tyrosine phosphorylation of Aha1 facilitates its binding to human Hsp90 [5], the cooperative action of these posttranslational modifications (PTMs) and their impact on protein interaction warrants further investigation

  • It is possible to identify regulatory amino acids that are subject to PTMs and impact the conformational dynamics and ATPase activity of Hsp90 both in vitro and in vivo [6]

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Summary

MEETING REPORT

Giorgio Colombo (University of Pavia, Italy) demonstrated the use of computational design in deciphering the chaperone code Using this approach, it is possible to identify regulatory amino acids that are subject to PTMs and impact the conformational dynamics and ATPase activity of Hsp both in vitro and in vivo [6]. Dimitra Bourboulia (SUNY Upstate Medical University, USA) discussed how secreted kinase signaling could impact extracellular Hsp (eHsp90) chaperone function She showed that the first secretory eHsp co-chaperone TIMP2 [8], an endogenous inhibitor of angiogenesis and regulator of MMP2 activity, is phosphorylated by secreted c-Src tyrosine kinase [9]. Following on from this, Matthias Truttmann (University of Michigan, USA) provided evidence that AMPylation of BiP in C. elegans does not alter animal survival, it does reduce Aβ toxicity, an effect that can be mimicked by directly silencing Hsp chaperones Hsp , and 4 simultaneously [25]

Extending the chaperone code
Findings
Concluding remarks
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