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22.08.2022: Publication Alert - The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes

Biological membranes present a unique barrier, critical for the compartmentalization of a living cell from its environment. Factors compromising the structure of membranes could result in serious consequences for the integrity of a cell. Thus, characterization of the mechanisms for maintaining and repairing cell membrane structures is crucial for a deeper understanding of cellular physiology, stress responses, and the development of membrane-associated pathologies.


Small heat shock proteins (sHSPs) have been demonstrated to interact with lipids and modulate the physical state of membranes across species. Through these interactions, sHSPs contribute to the maintenance of membrane integrity. HSPB1 is a major sHSP in mammals, but its lipid interaction profile has so far been unexplored. In this study, we characterized the interaction between HSPB1 and phospholipids. HSPB1 not only associated with membranes via membrane-forming lipids, but also showed a strong affinity towards highly fluid membranes. It participated in the modulation of the physical properties of the interacting membranes by altering rotational and lateral lipid mobility. In addition, the in vivo expression of HSPB1 greatly affected the phase behavior of the plasma membrane under membrane fluidizing stress conditions. In light of our current findings, we propose a new function for HSPB1 as a membrane chaperone.

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