Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

• DOI: 10.1007/s12192-021-01210-8
• Publication Date: 2021-05-18T07:02:32Z
• Authors: Paulo R. Dores-Silva; David M. Cauvi; Amanda L.S. Coto; Noeli S.M. Silva; Júlio C. Borges; Antonio De Maio
• Keywords: 0301 basic medicine; 570; Original Paper; Membranes; Cardiolipins; Cell Membrane; HSC70 Heat-Shock Proteins; 610; Hsp70; 03 medical and health sciences; Chaperones; HSP90AA1; Liposomes; HSPA8; Humans; HSP70 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; HSPA1A; Heat-Shock Proteins; Heat-Shock Response; Phospholipids; Molecular Chaperones

Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array biological processes. In addition, HSP play important role protection from various environmental stresses. part a large family different molecular mass polypeptides, displaying expression patterns, subcellular localizations, and diversity functions. An unexpected observation was detection on cell surface. Subsequent studies have demonstrated that ability to interact penetrate lipid bilayers process initiated recognition phospholipid heads, followed conformational changes, membrane insertion, oligomerization. present study, we described interaction HSPA8 (HSC70), constitutive cytosolic member HSP70 family, with membranes. showed high selectivity negatively charged phospholipids, such as phosphatidylserine cardiolipin, low affinity phosphatidylcholine. Membrane insertion mediated spontaneous driven increases entropy diminished presence ADP or ATP. Finally, capable driving into bilayer HSP90 does not display any biding capacity itself. This suggests may act chaperone.