Cristae junction as a fundamental switchboard for mitochondrial ion signaling and bioenergetics. (January 2022)
- Record Type:
- Journal Article
- Title:
- Cristae junction as a fundamental switchboard for mitochondrial ion signaling and bioenergetics. (January 2022)
- Main Title:
- Cristae junction as a fundamental switchboard for mitochondrial ion signaling and bioenergetics
- Authors:
- Gottschalk, Benjamin
Madreiter-Sokolowski, Corina T.
Graier, Wolfgang F. - Abstract:
- Highlights: Cristae junction represent a diffusion barrier for Ca 2+ and H + . Permeability of the cristae junction for ions, proteins and metabolites is controlled by OPA1 and MICU1. Ca 2+ dependent cristae junction regulation is mediated by MICU1. Disruption of the cristae junction result in Ca 2+ overload via constitutively active MCU located in the cristae membrane. OPA1 and MICU1 shape the cristae morphology to adapt to Ca 2+ signals and metabolic challenges. Abstract: OPA1 and MICU1 are both involved in the regulation of mitochondrial Ca 2+ uptake and the stabilization of the cristae junction, which separates the inner mitochondrial membrane into the interboundary membrane and the cristae membrane. In this mini-review, we focus on the synergetic control of OPA1 and MICU1 on the cristae junction that serves as a fundamental regulator of multiple mitochondrial functions. In particular, we point to the critical role of an adaptive cristae junction permeability in mitochondrial Ca 2+ signaling, spatial H + gradients and mitochondrial membrane potential, metabolic activity, and apoptosis. These characteristics bear on a distinct localization of the oxidative phosphorylation machinery, the Fo F1 -ATPase, and mitochondrial Ca 2+ uniporter (MCU) within sections of the inner mitochondrial membrane isolated by the cristae junction and regulated by proteins like OPA1 and MICU1. We specifically focus on the impact of MICU1-regulated cristae junction on the activity andHighlights: Cristae junction represent a diffusion barrier for Ca 2+ and H + . Permeability of the cristae junction for ions, proteins and metabolites is controlled by OPA1 and MICU1. Ca 2+ dependent cristae junction regulation is mediated by MICU1. Disruption of the cristae junction result in Ca 2+ overload via constitutively active MCU located in the cristae membrane. OPA1 and MICU1 shape the cristae morphology to adapt to Ca 2+ signals and metabolic challenges. Abstract: OPA1 and MICU1 are both involved in the regulation of mitochondrial Ca 2+ uptake and the stabilization of the cristae junction, which separates the inner mitochondrial membrane into the interboundary membrane and the cristae membrane. In this mini-review, we focus on the synergetic control of OPA1 and MICU1 on the cristae junction that serves as a fundamental regulator of multiple mitochondrial functions. In particular, we point to the critical role of an adaptive cristae junction permeability in mitochondrial Ca 2+ signaling, spatial H + gradients and mitochondrial membrane potential, metabolic activity, and apoptosis. These characteristics bear on a distinct localization of the oxidative phosphorylation machinery, the Fo F1 -ATPase, and mitochondrial Ca 2+ uniporter (MCU) within sections of the inner mitochondrial membrane isolated by the cristae junction and regulated by proteins like OPA1 and MICU1. We specifically focus on the impact of MICU1-regulated cristae junction on the activity and distribution of MCU within the complex ultrastructure of mitochondria. Graphical abstract: Image, graphical abstract … (more)
- Is Part Of:
- Cell calcium. Volume 101(2022)
- Journal:
- Cell calcium
- Issue:
- Volume 101(2022)
- Issue Display:
- Volume 101, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 101
- Issue:
- 2022
- Issue Sort Value:
- 2022-0101-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-01
- Subjects:
- Calcium -- Metabolism -- Periodicals
Vertebrates -- Physiology -- Periodicals
Calcium -- Physiological effect -- Periodicals
Cell physiology -- Periodicals
Calcium in the body -- Periodicals
572.516 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01434160 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.ceca.2021.102517 ↗
- Languages:
- English
- ISSNs:
- 0143-4160
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3097.724000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 20464.xml