Functional analysis of layilin by identification of layilin-interacting proteins using proximity-dependent biotin identification

2020 Fiscal Year Final Research Report

• Project/Area Number: 19K15752
• Research Category: Grant-in-Aid for Early-Career Scientists
• Allocation Type: Multi-year Fund
• Review Section: Basic Section 38030:Applied biochemistry-related
• Research Institution: St. Marianna University School of Medicine
• Principal Investigator: Tsutiya Atsuhiro 聖マリアンナ医科大学, 医学部, 助教 (30790068)
• Project Period (FY): 2019-04-01 – 2021-03-31
• Keywords: ライリン / 近位依存性ビオチン標識 / ミトコンドリア

Outline of Final Research Achievements

Proximity-dependent biotin identification (BioID) followed by 2D Western blot showed 17 protein spots that were likely bound to layilin. We analyzed them by mass spectrometry and identified several candidate proteins. On the other hand, we analyzed subcellular localization of layilin using double immunocytochemistory and found that layilin localized to mitochondria or in their close proximity. In addition, we revealed that layilin promotes mitochondrial fission by cyclin-dependent kinase 1 (CDK1) and dynamin-related protein 1 (DRP1) activation.

Free Research Field

生化学　細胞生物学

Academic Significance and Societal Importance of the Research Achievements

これまでライリンが結合するタンパク質は、一部の細胞骨格タンパク質を除いて不明であった。本研究はライリンと細胞質中で結合する新規候補タンパク質を複数同定できたという点で学術的意義がある。また本研究は、これまでヒアルロン酸の受容体とされていたライリンについて、「ミトコンドリアの切断促進」という新たな細胞内での機能を見出したという点で学術的意義がある。