title: Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.
abstract: The membrane binding properties of cytosolic and mitochondrial creatine kinase isoenzymes are reviewed in this article. Differences between both dimeric and octameric mitochondrial creatine kinase (Mi-CK) attached to membranes and the unbound form are elaborated with respect to possible biological function. The formation of crystalline mitochondrial inclusions under pathological conditions and its possible origin in the membrane attachment capabilities of Mi-CK are discussed. Finally, the implications of these results on mitochondrial energy transduction and structure are presented.
authors.affiliation: Swiss Federal Institute of Technology, Institute of Cell Biology, ETH Zürich-Hönggerberg.
authors.forename: O
authors.initials: O
authors.lastname: Stachowiak
authors.forename: U
authors.initials: U
authors.lastname: Schlattner
authors.forename: M
authors.initials: M
authors.lastname: Dolder
authors.forename: T
authors.initials: T
authors.lastname: Wallimann
mesh_terms: D001665:Binding Sites / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D003402:Creatine Kinase / Q000737:chemistry*; D007527:Isoenzymes; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology* / Q000502:physiology; D008958:Models, Molecular; D011485:Protein Binding / Q000502:physiology; D011487:Protein Conformation
chemical_list: D007527:Isoenzymes; D003402:Creatine Kinase