The EF-Hand Ca2+ Binding Protein MICU Choreographs Mitochondrial Ca2+ Dynamics in Arabidopsis. Issue 11 (3rd November 2015)
- Record Type:
- Journal Article
- Title:
- The EF-Hand Ca2+ Binding Protein MICU Choreographs Mitochondrial Ca2+ Dynamics in Arabidopsis. Issue 11 (3rd November 2015)
- Main Title:
- The EF-Hand Ca2+ Binding Protein MICU Choreographs Mitochondrial Ca2+ Dynamics in Arabidopsis
- Authors:
- Wagner, Stephan
Behera, Smrutisanjita
De Bortoli, Sara
Logan, David C.
Fuchs, Philippe
Carraretto, Luca
Teardo, Enrico
Cendron, Laura
Nietzel, Thomas
Füßl, Magdalena
Doccula, Fabrizio G.
Navazio, Lorella
Fricker, Mark D.
Van Aken, Olivier
Finkemeier, Iris
Meyer, Andreas J.
Szabò, Ildikò
Costa, Alex
Schwarzländer, Markus - Abstract:
- Abstract : The mitochondrial Ca 2+ uptake protein At-MICU shapes mitochondrial Ca 2+ dynamics, providing molecular in vivo evidence for the existence and function of a mitochondrial uniporter complex in plants. Abstract: Plant organelle function must constantly adjust to environmental conditions, which requires dynamic coordination. Ca 2+ signaling may play a central role in this process. Free Ca 2+ dynamics are tightly regulated and differ markedly between the cytosol, plastid stroma, and mitochondrial matrix. The mechanistic basis of compartment-specific Ca 2+ dynamics is poorly understood. Here, we studied the function of At-MICU, an EF-hand protein of Arabidopsis thaliana with homology to constituents of the mitochondrial Ca 2+ uniporter machinery in mammals. MICU binds Ca 2+ and localizes to the mitochondria in Arabidopsis. In vivo imaging of roots expressing a genetically encoded Ca 2+ sensor in the mitochondrial matrix revealed that lack of MICU increased resting concentrations of free Ca 2+ in the matrix. Furthermore, Ca 2+ elevations triggered by auxin and extracellular ATP occurred more rapidly and reached higher maximal concentrations in the mitochondria of micu mutants, whereas cytosolic Ca 2+ signatures remained unchanged. These findings support the idea that a conserved uniporter system, with composition and regulation distinct from the mammalian machinery, mediates mitochondrial Ca 2+ uptake in plants under in vivo conditions. They further suggest that MICUAbstract : The mitochondrial Ca 2+ uptake protein At-MICU shapes mitochondrial Ca 2+ dynamics, providing molecular in vivo evidence for the existence and function of a mitochondrial uniporter complex in plants. Abstract: Plant organelle function must constantly adjust to environmental conditions, which requires dynamic coordination. Ca 2+ signaling may play a central role in this process. Free Ca 2+ dynamics are tightly regulated and differ markedly between the cytosol, plastid stroma, and mitochondrial matrix. The mechanistic basis of compartment-specific Ca 2+ dynamics is poorly understood. Here, we studied the function of At-MICU, an EF-hand protein of Arabidopsis thaliana with homology to constituents of the mitochondrial Ca 2+ uniporter machinery in mammals. MICU binds Ca 2+ and localizes to the mitochondria in Arabidopsis. In vivo imaging of roots expressing a genetically encoded Ca 2+ sensor in the mitochondrial matrix revealed that lack of MICU increased resting concentrations of free Ca 2+ in the matrix. Furthermore, Ca 2+ elevations triggered by auxin and extracellular ATP occurred more rapidly and reached higher maximal concentrations in the mitochondria of micu mutants, whereas cytosolic Ca 2+ signatures remained unchanged. These findings support the idea that a conserved uniporter system, with composition and regulation distinct from the mammalian machinery, mediates mitochondrial Ca 2+ uptake in plants under in vivo conditions. They further suggest that MICU acts as a throttle that controls Ca 2+ uptake by moderating influx, thereby shaping Ca 2+ signatures in the matrix and preserving mitochondrial homeostasis. Our results open the door to genetic dissection of mitochondrial Ca 2+ signaling in plants. … (more)
- Is Part Of:
- The Plant Cell. Volume 27:Issue 11(2015)
- Journal:
- The Plant Cell
- Issue:
- Volume 27:Issue 11(2015)
- Issue Display:
- Volume 27, Issue 11 (2015)
- Year:
- 2015
- Volume:
- 27
- Issue:
- 11
- Issue Sort Value:
- 2015-0027-0011-0000
- Page Start:
- 3190
- Page End:
- 3212
- Publication Date:
- 2015-11-03
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00509 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16357.xml