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

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.
Type de document :
Article dans une revue
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2001, 276 (51), pp.48027-30. 〈10.1074/jbc.M106524200〉
Liste complète des métadonnées

http://www.hal.inserm.fr/inserm-00390835
Contributeur : Sarah Hamant <>
Soumis le : mardi 2 juin 2009 - 19:04:35
Dernière modification le : mardi 7 juillet 2009 - 10:16:43

Lien texte intégral

Identifiants

Collections

Citation

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, American Society for Biochemistry and Molecular Biology, 2001, 276 (51), pp.48027-30. 〈10.1074/jbc.M106524200〉. 〈inserm-00390835〉

Partager

Métriques

Consultations de la notice

393