Journal
JOURNAL OF CELL SCIENCE
Volume 131, Issue 9, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.210500
Keywords
L1CAM; Mitochondria; Mitochondrial metabolism; Respiratory chain; Complex I
Categories
Funding
- Keck Center of the Department of Cell Biology and Neuroscience at Rutgers
- State University of New Jersey
- Li Ka Shing Foundation at Shantou University Medical College
Ask authors/readers for more resources
The cell adhesion molecule L1 (also known as L1CAM) 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 all lead to reduced mitochondrial complex I activity, and 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available