Unravelling the structure of toxic protein aggregates in situ

− この都医学研セミナーは終了しました。 −

演者 Rubén Fernández-Busnadiego
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry(Project Group leader)
会場 東京都医学総合研究所 2階講堂
日時 平成30年3月13日(火)16:30~
世話人 田中 啓二 (東京都医学総合研究所 所長)
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Protein aggregation is a hallmark of many neurodegenerative diseases, including Huntington’s, Parkinson’s and amyotrophic lateral sclerosis. However, the mechanisms linking aggregation to neurotoxicity remain poorly understood, partly because only limited information is available on the native structure of protein aggregates inside cells. We address this pressing issue utilizing the latest developments in cryo-electron tomography (cryo-ET). We prepare thin lamellas of vitrified cells containing protein aggregates using cryo-focused ion beam, and subsequently image them in three dimensions by cryo-ET. This allows us to analyse aggregate structure within pristinely preserved cellular environments and at molecular resolution [1, 2]. Here, I will discuss how our latest results shed new light into the cellular mechanisms of neurodegeneration.