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Determining the Solution Structure of the Drp1 and its Role in the Assembly of the Mitochondrial Fission Machinery

Mitochondria are double-membrane organelles found in eukaryotic cells and are responsible for cellular metabolism [1]. These organelles undergo fission and fusion in response to cellular stress, and several proteins have been identified to be critical to these processes [2-4]. Dynamin-related protein 1 (Drp1) is the key protein required for mitochondrial fission [1, 5]. Drp1 is comprised of three conserved domains common to the dynamin family of proteins, the GTPase, middle, and the GTPase effector domain (GED) [6, 7]. In addition, there is a variable domain (VD), which is intrinsically disordered, that we have shown serves a regulatory function [6-8]. Like dynamin in endocytosis, Drp1 forms dimers [5] that polymerize into helical structures around lipid templates [9]. An atomic structure of Drp1 was resolved using crystallography as part of a larger tetramer in the crystal lattice [10]. However, a mutated construct lacking the VD was used to aid crystallization, and it is unclear whether these changes impact the solution structure of the Drp1. Knowing the native structure of Drp1 before functional polymerization will provide fundamental insight into the early steps of the mitochondrial fission mechanism. This insight could then be used to probe mitochondria dysfunction as it relates to human disease such as neurodegenerative disorders including Huntington’s, Parkinson’s, and Alzheimer’s diseases and amyotrophic lateral sclerosis [11].