The α-crystallin chaperones undergo a quasi-ordered co-aggregation process in response to saturating client interaction.

ABSTRACT: Small heat shock proteins (sHSPs) are ATP-independent chaperones vital to cellular proteostasis, preventing protein aggregation events linked to various human diseases including cataract. The α-crystallins, αA-crystallin (αAc) and αB-crystallin (αBc), represent archetypal sHSPs that exhibit complex polydispersed oligomeric assemblies and rapid subunit exchange dynamics. Yet, our understanding of how this plasticity contributes to chaperone function remains poorly understood. This study investigates structural changes in αAc and αBc during client sequestration under varying degree of chaperone saturation. Using biochemical and biophysical analyses combined with single-particle electron microscopy (EM), we examined αAc and αBc in their apo-states and at various stages of client-induced co-ag

SUBMITTER: Miller AP 

PROVIDER: S-EPMC10462102 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature