Abstract
Mitochondrial creatine kinase (mtCK) binding to the mitochondrial inner membrane largely determines its biological functions in cellular energy homeostasis, mitochondrial physiology, and dynamics. The membrane binding mechanism is, however, not completely understood. Recent data suggest that a hydrophobic component is involved in mtCK binding to cardiolipin at the outer face of the inner mitochondrial membrane, in addition to the well known electrostatically driven process. In this manuscript, using an electrochemical method derived from alternating current polarography for differential capacity measurements, we distinctly reveal that protein–cardiolipin interaction has a two-step mechanism. For short incubation time, protein adsorption to the phospholipid charged headgroup was the only process detected, whereas on a longer time scale evidence of protein insertion was observed.
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Abbreviations
- CK:
-
Creatine kinase
- mtCK:
-
Mitochondrial creatine kinase
- CL:
-
Cardiolipin
- ac:
-
Alternating current
- C :
-
Differential capacity
- E :
-
Electrical potential
- pzc:
-
Potential of zero charge
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Acknowledgments
We are very grateful to Dr J. Clavilier for very fruitful suggestions and discussions. We acknowledge funding from University Lyon 1, CNRS, Région Rhône-Alpes and Agence Nationale de la Recherche.
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Maniti, O., Lecompte, MF., Marcillat, O. et al. Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion. Eur Biophys J 39, 1649–1655 (2010). https://doi.org/10.1007/s00249-010-0600-4
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DOI: https://doi.org/10.1007/s00249-010-0600-4