Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Veneto Institute of Molecular Medicine · Dulbecco Telethon Institute · +3 more institutions
Abstract
Changes in mitochondrial morphology that occur during cell cycle, differentiation, and death are tightly regulated by the balance between fusion and fission processes. Excessive fragmentation can be caused by inhibition of the fusion machinery and is a common consequence of dysfunction of the organelle. Here, we show a role for calcineurin-dependent translocation of the profission dynamin related protein 1 (Drp1) to mitochondria in dysfunction-induced fragmentation. When mitochondrial depolarization is associated with sustained cytosolic Ca(2+) rise, it activates the cytosolic phosphatase calcineurin that normally interacts with Drp1. Calcineurin-dependent dephosphorylation of Drp1, and in particular of its…
Citation impact
- FWCI
- 16.70
- Percentile
- 100%
- References
- 35
Authors
7- GMGrazia M. CereghettiCorresponding
Veneto Institute of Molecular Medicine, Dulbecco Telethon Institute
- ASAlessandra Stangherlin
Veneto Institute of Molecular Medicine, Dulbecco Telethon Institute
- OMOlga Martins de Brito
Veneto Institute of Molecular Medicine, Dulbecco Telethon Institute
- CCChuang‐Rung Chang
National Institutes of Health, National Institute of Neurological Disorders and Stroke
- CBCraig Blackstone
National Institutes of Health, National Institute of Neurological Disorders and Stroke
Topics & keywords
- Cell biology
- Dephosphorylation
- Mitochondrial fission
- Mitochondrion
- Biology
- Calcineurin
- Cytosol
- mitochondrial fusion