The Centre of New Technologies invites to a seminar by
Jeff Noel, AG Daumke
Venue: Centre of New Technologies, Banacha 2C, Lecture Hall 0142 (Ground floor)
Living cells are surrounded by lipid membranes that undergo fusion and fission with smaller membrane compartments to allow for materials to be trafficked in and out of the cell. A frontier of molecular biology is to understand the spatiotemporal membrane-protein interactions that enable these membrane remodelling processes such as such as endocytosis and mitochondrial fission. Dynamin is the best-characterized member of the dynamin-related protein family, proteins that polymerize around tubular membranes into helical geometries and lead to fission of these tubes in a GTP dependent manner. Crystallography and cryo-EM have provided rich structural information about the shape of assembled membrane-dynamin complexes and have suggested a putative nucleotide-dependent conformational change. Amazingly, the dynamin polymer is a fusion of a structural (e.g. actin) and motor domain (e.g. myosin), and, therefore, how the motor domains across helical turns are able to “walk” on each other and create the largest torques in the body (>1000 pN*nm) is a fascinating problem.
I will discuss the development of a coarse-grained model of the motor function that is derived from various atomistic simulations and FRET experiments on single motor domains performed in our lab.