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    The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes

    Year: 2022

    Journal: Int. J. Mol. Sci., Volume 23, JUL

    Authors: Csoboz, Balint; Gombos, Imre; Kota, Zoltan; Dukic, Barbara; Klement, Eva; Varga-Zsiros, Vanda; Lipinszki, Zoltan; Pali, Tibor; Vigh, Laszlo; Torok, Zsolt

    Organizations: Hungarian Basic Research Fund [OTKA ANN 132280]; Hungarian Academy of Sciences (Lendulet Grant) [LP2017-7/2017]; EU [739593]

    Keywords: small HSP; lipid-protein interaction; membrane chaperone; membrane fluidity; stress response

    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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