ZB 10 - Soft Condensed Matter (R. Holyst)

Insight into the fission mechanism by quantitative characterization of Drp1 protein distribution in the living cell

Author(s): Michalska, Bernadeta Maria and Kwapiszewska, Karina and Szczepanowska, and Kalwarczyk, Tomasz and Patalas-Krawczyk, Paulina and Krzysztof and Holyst, Robert and Duszynski, Jerzy and Szymanski, Jedrzej
Title: Insight into the fission mechanism by quantitative characterization of Drp1 protein distribution in the living cell
Abstract: One of the main players in the process of mitochondrial fragmentation is protein 1 (Drp1), which assembles into a helical structure on the mitochondria and facilitates fission. The mechanism is still poorly understood and detailed information oligomeric form of Drp1, its cellular distribution and the of the fission complex is missing. To estimate oligomeric forms of in the cytoplasm and on the mitochondria, we performed a analysis of Drp1 diffusion and distribution in gene-edited cell lines. This paper provides an insight into the fission based on the quantitative description of Drp1 cellular We found that approximately half of the endogenous pool remained in the cytoplasm, predominantly in a tetrameric at a concentration of 28 +/- 9 nM. The Drp1 mitochondrial pool many different oligomeric states with equilibrium distributions could be described by isodesmic supramolecular polymerization with Kd of 31 +/- 10 nM. We estimated the average number of Drp1 molecules the functional fission complex to be approximately 100, not more than 14\% of all Drp1 oligomers. We showed that upregulated fission induced by niclosamide is accompanied by an increase in the number of large Drp1 oligomers.
Journal: SCIENTIFIC REPORTS
Publisher: NATURE PUBLISHING GROUP
Addres: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
Volume: 8
ID: ISI:000433061300004
Year: 2018
DOI: 10.1038/s41598-018-26578-z