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- W2797369529 abstract "The cell adhesion molecule L1 plays important roles in the mammalian nervous system under physiological and pathological conditions. We have previously reported that proteolytic cleavage of L1 by myelin basic protein leads to the generation of a 70 kDa transmembrane L1 fragment (L1-70) that promotes neuronal migration and neuritogenesis. Here, we provide evidence that L1-70 is imported from the cytoplasm into mitochondria. Genetic ablation of L1, inhibition of mitochondrial import of L1-70 or prevention of myelin basic protein-mediated generation of L1-70 lead to reduced mitochondrial complex I activity, impaired mitochondrial membrane potential, fusion, fission, and motility as well as increased retrograde transport. We identified NADH dehydrogenase ubiquinone flavoprotein 2 as a binding partner for L1, suggesting that L1-70 interacts with this complex I subunit to regulate complex I activity. The results of our study provide insights into novel functions of L1 in mitochondrial metabolism and cellular dynamics. These functions are likely to ameliorate the consequences of acute nervous system injuries and chronic neurodegenerative diseases." @default.
- W2797369529 created "2018-04-24" @default.
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- W2797369529 date "2018-01-01" @default.
- W2797369529 modified "2023-09-24" @default.
- W2797369529 title "A fragment of adhesion molecule L1 is imported into mitochondria and regulates mitochondrial metabolism and trafficking" @default.
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- W2797369529 doi "https://doi.org/10.1242/jcs.210500" @default.
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