ArticleBiophysical journal2012
A biophysical model of the mitochondrial ATP-Mg/P(i) carrier.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Agent-based modeling of neuronal mitochondrial dynamics using intrinsic variables of individual mitochondria.iScience · 2025Article
- A pair of transporters controls mitochondrial ZnProtein & cell · 2022Article
- Mitochondrial CaPharmacology & therapeutics · 2018Review
- Molecular regulation of MCU: Implications in physiology and disease.Cell calcium · 2018Review
- Solute carrier 41A3 encodes for a mitochondrial Mg(2+) efflux system.Scientific reports · 2016Article
- Determination of the catalytic mechanism for mitochondrial malate dehydrogenase.Biophysical journal · 2015Article
- SLC25A23 augments mitochondrial Ca²⁺ uptake, interacts with MCU, and induces oxidative stress-mediated cell death.Molecular biology of the cell · 2014Article
- A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport.Structure (London, England : 1993) · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial adenine nucleotide (AdN) content is regulated through the Ca(2+)-activated, electroneutral ATP-Mg/P(i) carrier (APC). The APC is a protein in the mitochondrial carrier super family that localizes to the inner mitochondrial membrane (IMM). It is known to modulate a number of processes that depend on mitochondrial AdN content, such as gluconeogenesis, protein synthesis, and citrulline synthesis. Despite this critical role, a kinetic model of the underlying mechanism has not been developed and validated. Here, a biophysical model of the APC is developed that is thermodynamically balanced and accurately reproduces a number of reported data sets from isolated rat liver and rat kidney mitochondria. The model is based on an ordered bi-bi mechanism for heteroexchange of ATP and P(i) and includes homoexchanges of ATP and P(i) to explain both the initial rate and time course data on ATP and P(i) transport via the APC. The model invokes seven kinetic parameters regarding the APC mechanism and three parameters related to matrix pH regulation by external P(i). These parameters are estimated based on 19 independent data curves; the estimated parameters are validated using six additional data curves. The model takes into account the effects of pH, Mg(2+), and Ca(2+) on ATP and P(i) transport via the APC, and supports the conclusion that the pH gradient across the IMM serves as the primary driving force for AdN uptake or efflux. Moreover, computer simulations demonstrate that extramatrix Ca(2+) modulates the turnover rate of the APC and not the binding affinity of ATP, as previously suggested.
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