MI
Miho Iijima
  • Department of Cell Biology, Johns Hopkins University School of Medicine, USA
Research fields
  • Biochemistry
Assay to Measure Interactions between Purified Drp1 and Synthetic Liposomes
Authors:  Yoshihiro Adachi, Kie Itoh, Miho Iijima and Hiromi Sesaki, date: 05/05/2017, view: 9707, Q&A: 0
A mitochondrion is a dynamic intracellular organelle that actively divides and fuses to control its size, number and shape in cells. A regulated balance between mitochondrial division and fusion is fundamental to the function, distribution and turnover of mitochondria (Roy et al., 2015). Mitochondrial division is mediated by dynamin-related protein 1 (Drp1), a mechano-chemical GTPase that constricts mitochondrial membranes (Tamura et al., 2011). Mitochondrial membrane lipids such as phosphatidic acid and cardiolipin bind Drp1, and Drp1-phospholipid interactions provide key regulatory mechanisms for mitochondrial division (Montessuit et al., 2010; Bustillo-Zabalbeitia et al., 2014; Macdonald et al., 2014; Stepanyants et al., 2015; Adachi et al., 2016). Here, we describe biochemical experiments that quantitatively measure interactions of Drp1 with lipids using purified recombinant Drp1 and synthetic liposomes with a defined set of phospholipids. This assay makes it possible to define the specificity of protein-lipid interaction and the role of the head group and acyl chains.
We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.