Quantitative analysis of proteostasis disruption following siRNA-mediated HSP70 depletion in HeLa cells

Introduction

Heat shock protein 70 (HSP70) is a central molecular chaperone that maintains proteostasis by supporting protein folding, preventing protein aggregation, and coordinating cellular stress responses. Dysregulation of HSP70 has been associated with cancer progression, neurodegenerative disorders, and aging-related proteotoxicity. However, many experimental approaches rely on chemical inhibition or stress-inducing conditions that may introduce additional confounding effects. This study aimed to investigate the proteostatic consequences of HSP70 depletion in the absence of stress-inducing chemical inhibitors.