Prohibitin levels regulate OMA1 activity and turnover in neurons

The GTPase OPA1 and the AAA-protease OMA1 serve well-established roles in mitochondrial stress responses and mitochondria-initiated cell death. In addition to its role in mitochondrial membrane fusion, cristae structure, and bioenergetic function, OPA1 controls apoptosis by sequestering cytochrome c...

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Veröffentlicht in:Cell death and differentiation 2020-06, Vol.27 (6), p.1896-1906
Hauptverfasser: Anderson, Corey J., Kahl, Anja, Fruitman, Hannah, Qian, Liping, Zhou, Ping, Manfredi, Giovanni, Iadecola, Costantino
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container_end_page 1906
container_issue 6
container_start_page 1896
container_title Cell death and differentiation
container_volume 27
creator Anderson, Corey J.
Kahl, Anja
Fruitman, Hannah
Qian, Liping
Zhou, Ping
Manfredi, Giovanni
Iadecola, Costantino
description The GTPase OPA1 and the AAA-protease OMA1 serve well-established roles in mitochondrial stress responses and mitochondria-initiated cell death. In addition to its role in mitochondrial membrane fusion, cristae structure, and bioenergetic function, OPA1 controls apoptosis by sequestering cytochrome c (cyt c) in mitochondrial cristae. Cleavage of functional long OPA1 (L-OPA1) isoforms by OMA1 inactivates mitochondrial fusion and primes apoptosis. OPA1 cleavage is regulated by the prohibitin (PHB) complex, a heteromeric, ring-shaped mitochondrial inner membrane scaffolding complex composed of PHB1 and PHB2. In neurons, PHB plays a protective role against various stresses, and PHB deletion destabilizes OPA1 causing neurodegeneration. While deletion of OMA1 prevents OPA1 destabilization and attenuates neurodegeneration in PHB2 KO mice, how PHB levels regulate OMA1 is still unknown. Here, we investigate the effects of modulating neuronal PHB levels on OMA1 stability and OPA1 cleavage. We demonstrate that PHB promotes OMA1 turnover, effectively decreasing the pool of OMA1. Further, we show that OMA1 binds to cardiolipin (CL), a major mitochondrial phospholipid. CL binding promotes OMA1 turnover, as we show that deleting the CL-binding domain of OMA1 decreases its turnover rate. Since PHB is known to stabilize CL, these data suggest that PHB modulates OMA1 through CL. Furthermore, we show that PHB decreases cyt c release induced by tBID and attenuates caspase 9 activation in response to hypoxic stress in neurons. Taken together, our results suggest that PHB-mediated CL stabilization regulates stress responses and cell death through OMA1 turnover and cyt c release.
doi_str_mv 10.1038/s41418-019-0469-4
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Further, we show that OMA1 binds to cardiolipin (CL), a major mitochondrial phospholipid. CL binding promotes OMA1 turnover, as we show that deleting the CL-binding domain of OMA1 decreases its turnover rate. Since PHB is known to stabilize CL, these data suggest that PHB modulates OMA1 through CL. Furthermore, we show that PHB decreases cyt c release induced by tBID and attenuates caspase 9 activation in response to hypoxic stress in neurons. Taken together, our results suggest that PHB-mediated CL stabilization regulates stress responses and cell death through OMA1 turnover and cyt c release.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31819158</pmid><doi>10.1038/s41418-019-0469-4</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
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subjects 13/1
13/106
42/109
42/35
42/44
631/378
64/60
692/699/375
82/80
Apoptosis
Biochemistry
Biomedical and Life Sciences
Cardiolipin
Caspase-9
Cell Biology
Cell Cycle Analysis
Cell death
Cellular stress response
Cristae
Cytochrome c
Diphosphatidylglycerol
Guanosine triphosphatases
Hypoxia
Isoforms
Life Sciences
Membrane fusion
Mitochondria
Neurodegeneration
Phospholipids
Prohibitin
Stem Cells
Structure-function relationships
title Prohibitin levels regulate OMA1 activity and turnover in neurons
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