Mitochondrial dynamics: the dynamin superfamily and execution by collusion

Abstract

Distinct dynamin superfamily GTPases catalyze the constant fission and fusion of the elaborate mitochondrial networks that navigate the eukaryotic cytoplasm. Long believed to be the singular handiwork of dynamin-related protein 1 (Drp1), a cytosolic family member that transiently localizes to the mitochondrial surface, the execution of mitochondrial fission is now arguably believed to entail membrane remodeling events that are initiated upstream of Drp1 by ER-associated cytoskeletal networks and completed downstream by the prototypical dynamin, dynamin 2 (Dyn2). Recent developments in the field have also placed a sharp focus on the membrane microenvironment around the division apparatus and the potential facilitatory role of specific lipids in mitochondrial fission. Here, I will review current progress, as well as highlight the most visible gaps in knowledge, in elucidating the varied functions of the dynamin superfamily in the coordinated events of mitochondrial fission and fusion. The essential roles of protein and lipid cofactors are also highlighted.