Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.

IF 4.3 3区材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC ACS Applied Electronic Materials Pub Date : 2023-11-01 Epub Date: 2023-11-25 DOI:10.1007/s12192-023-01394-1

Milene N O Moritz, Paulo R Dores-Silva, Amanda L S Coto, Heloísa S Selistre-de-Araújo, Andrei Leitão, David M Cauvi, Antonio De Maio, Serena Carra, Júlio Cesar Borges

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Abstract

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.

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人hsp70 -护航蛋白1 (hHep1)与带负电荷的脂质双分子层和细胞膜相互作用。

人hsp70 -护航蛋白1 (hHep1)是一种辅助线粒体HSPA9功能和稳定性的协同伴侣。与HSPA9类似，hHep1位于线粒体外，可与脂质体相互作用。在这项研究中，我们进一步研究了hHep1与带负电荷的脂质体之间的相互作用以及与细胞膜的相互作用的结构和热力学行为。我们的研究结果表明，hHep1与磷脂酰丝氨酸和心磷脂形成的脂质体外周相互作用，并保持部分结构，对两者表现出相似的亲和力。此外，重组hHep1加入细胞膜后，以剂量依赖的方式被细胞掺入。有趣的是，HSPA9与hHep1的结合改善了这些蛋白在脂质双分子层中的结合。这些结果表明，hHep1可以与存在于质膜中的脂质相互作用，表明这种合作伙伴蛋白在线粒体外的作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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