人类 HSP70-escort 蛋白 1(hHep1)与带负电荷的脂质双分子层和细胞膜相互作用。

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC ACS Applied Electronic Materials Pub Date : 2023-11-01 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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引用次数: 0

摘要

人类 Hsp70-escort 蛋白 1(hHep1)是一种辅助伴侣蛋白,有助于线粒体 HSPA9 的功能和稳定性。与 HSPA9 类似,hHep1 位于线粒体外,可与脂质体相互作用。在本研究中,我们进一步研究了 hHep1 与带负电荷脂质体相互作用的结构和热力学行为,以及与细胞膜的相互作用。我们的结果表明,hHep1 与磷脂酰丝氨酸和心磷脂形成的脂质体发生外围相互作用,并保持部分结构,对二者表现出相似的亲和力。此外,将重组 hHep1 加入细胞膜后,细胞会以剂量依赖的方式与之结合。有趣的是,HSPA9 与 hHep1 的结合提高了这些蛋白与脂质双分子层的结合。这些结果表明,hHep1也能与存在于质膜中的脂质相互作用,表明这种辅助伴侣蛋白在线粒体之外也能发挥作用。
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Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.

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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