Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium. - Archive ouverte HAL Access content directly
Journal Articles Journal of Biological Chemistry Year : 2001

Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium.

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Abstract

Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). Increased ionic strength reduced the binding of MtCK to porin, suggesting predominantly ionic interactions. By contrast, micromolar concentrations of Ca(2+) increased the amount of bound MtCK, indicating a physiological regulation of complex formation. No interaction of MtCK with reconstituted adenine nucleotide translocator was detectable in our experimental setup. The relevance of these findings for structure and function of mitochondrial contact sites is discussed.

Dates and versions

inserm-00390835 , version 1 (02-06-2009)

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Uwe Schlattner, Max Dolder, Theo Wallimann, Malgorzata Tokarska-Schlattner. Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium.. Journal of Biological Chemistry, 2001, 276 (51), pp.48027-30. ⟨10.1074/jbc.M106524200⟩. ⟨inserm-00390835⟩

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