Proteolytic regulation of mitochondrial dynamics

Spatiotemporal changes in the abundance, shape, arid cellular localization of the mitochondria] network, also known as mitochondrial dynamics, are now widely recognized to play a key role in mitochondrial and cellular physiology as well as disease states. This process involves coordinated remodeling of the outer and inner mitochondrial membranes by conserved dynamin-like guanosine triphosphatases and their partner molecules in response to various physiological and stress stimuli. Although the core machineries that mediate fusion and partitioning of the mitochondrial network have been extensively characterized, many aspects of their function and regulation are incompletely understood and only beginning to emerge. In the present review we briefly summarize current knowledge about how the key mitochondria] dynamics-mediating factors are regulated via selective proteolysis by mitochondria] and cellular proteolytic machineries.