期刊
JOURNAL OF CELL BIOLOGY
卷 220, 期 10, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201912077
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- Harvard NeuroDiscovery Center's Enhanced Neuroimaging Core (National Institute of Neurological Disorders and Stroke) [NS072030]
- Cellular Imaging Core Intellectual and Developmental Disabilities Research Center at Boston Children's Hospital (National Institutes of Health) [U54 HD090255]
- National Institutes of Health [R01 GM11200]
- National Institute of General Medical Sciences [R01 GM069808]
Glucose influx leads to O-GlcNAcylation of TRAK protein, which activates the mechanism of anchoring mitochondria to the F-actin cytoskeleton by FHL2. Disruption of F-actin restores mitochondrial movement arrested by TRAK.
Mitochondrial movement and distribution are fundamental to their function. Here we report a mechanism that regulates mitochondrial movement by anchoring mitochondria to the F-actin cytoskeleton. This mechanism is activated by an increase in glucose influx and the consequent O-GlcNAcylation of TRAK (Milton), a component of the mitochondrial motor-adaptor complex. The protein four and a half LIM domains protein 2 (FHL2) serves as the anchor. FHL2 associates with O-GlcNAcylated TRAK and is both necessary and sufficient to drive the accumulation of F-actin around mitochondria and to arrest mitochondrial movement by anchoring to F-actin. Disruption of F-actin restores mitochondrial movement that had been arrested by either TRAK O-GlcNAcylation or forced direction of FHL2 to mitochondria. This pathway for mitochondrial immobilization is present in both neurons and non-neuronal cells and can thereby adapt mitochondrial dynamics to changes in glucose availability.
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