Small heat shock proteins (sHSPs) are ubiquitous ATP-independent chaperone proteins involved in maintaining protein homeostasis in humans. Members of the small heat shock protein family, such as HSP27 and alpha-crystallin b, are known to be post-translationally O-GlcNAc modified in their C-terminal domains. Using semi-synthesis, we have found that such O-GlcNAcylation increases the ability of sHSPs to block protein aggregation. Mechanistically, this involves alterations in protein structure, suggesting that it will also affect protein-protein interactions and oligomerization. Here, I will present work exploring this possibility using a variety of techniques including proteomics and in vitro biochemistry.

Investigating the effects of O-GlcNAc on small heat shock protein structure, function, and interactions

ACS Spring 2022

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