Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.
Milene N O MoritzPaulo R Dores-SilvaAmanda L S CotoHeloísa S Selistre-de-AraújoAndrei LeitãoDavid M CauviAntonio De MaioSerena CarraJúlio César BorgesPublished in: Cell stress & chaperones (2023)
Human Hsp70-escort protein 1 (hHep1) is a cochaperone that assists in the function and stability of mitochondrial HSPA9. Similar to HSPA9, hHep1 is located outside the mitochondria and can interact with liposomes. In this study, we further investigated the structural and thermodynamic behavior of interactions between hHep1 and negatively charged liposomes, as well as interactions with cellular membranes. Our results showed that hHep1 interacts peripherally with liposomes formed by phosphatidylserine and cardiolipin and remains partially structured, exhibiting similar affinities for both. In addition, after being added to the cell membrane, recombinant hHep1 was incorporated by cells in a dose-dependent manner. Interestingly, the association of HSPA9 with hHep1 improved the incorporation of these proteins into the lipid bilayer. These results demonstrated that hHep1 can interact with lipids also present in the plasma membrane, indicating roles for this cochaperone outside of mitochondria.
Keyphrases
- heat shock protein
- drug delivery
- endothelial cells
- binding protein
- cell death
- fatty acid
- drug release
- heat shock
- induced apoptosis
- oxidative stress
- induced pluripotent stem cells
- pluripotent stem cells
- cell therapy
- amino acid
- protein protein
- cell cycle arrest
- signaling pathway
- endoplasmic reticulum
- molecular dynamics simulations
- mass spectrometry
- bone marrow