Moyamoya disease protein mysterin stabilizes lipid droplets
Daisuke Morito1, Munechika Sugihara2, Shiori Ainuki2, and Kazuhiro Nagata1,2 1Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, 603-8047, Japan 2Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8047, Japan
We have isolated mysterin as a susceptibility gene for cerebrovascular moyamoya disease (PLOS ONE, 2011), of which missense mutations are strongly associated with risk of a range of vascular disorders including moyamoya disease. Mysterin protein exerts mechanical ATPase (AAA+) and ubiquitin ligase activities, yet its biological relevance has remained virtually unknown (Sci Rep, 2014, 2015, 2017). We have recently identified that this protein is localized to lipid droplets (LDs), organelles formed throughout tissues for cytoplasmic fat storage, and stabilizes them by removing a neutral lipid lipase ATGL from their surface. We would like to discuss potential importance of mysterin in metabolic regulation and the pathophysiology of moyamoya disease.
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