α-突触核蛋白与 ATP 合酶的相互作用：从生理到病理的角色转换。
Interaction of α-Synuclein with ATP Synthase: Switching Role from Physiological to Pathological.
机构信息
Molecular and Structural Biophysics Laboratory, Department of Biochemistry , North-Eastern Hill University , Shillong 793022 , India.
CSIR-Indian Institute of Chemical Biology , 4, Raja SC Mallick Rd , Poddar Nagar, Jadavpur, Kolkata , West Bengal 700032 , India.
出版信息
ACS Chem Neurosci. 2019 Jan 16;10(1):16-17. doi: 10.1021/acschemneuro.8b00407. Epub 2018 Aug 22.
The most abundantly present protein found in Lewy bodies, which is the pathological hallmark of Parkinson's disease, is α-synuclein. Native monomeric α-synuclein is localized within mitochondria, interacts with ATP synthase subunit, and enhances ATP synthase efficiency and mitochondrial function. Recently, an advanced study shows that the interaction of α-synuclein oligomer with ATP synthase switches its role from physiological to pathological, which leads to mitochondrial dysfunction.
在路易体中发现的最丰富的蛋白质是α-突触核蛋白，它是帕金森病的病理标志。天然单体α-突触核蛋白位于线粒体内部，与 ATP 合酶亚基相互作用，增强 ATP 合酶的效率和线粒体功能。最近，一项深入研究表明，α-突触核蛋白寡聚体与 ATP 合酶的相互作用使其作用从生理状态转变为病理状态，导致线粒体功能障碍。
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