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Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: Implications for cellular function and mitochondrial structure

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Book cover Bioenergetics of the Cell: Quantitative Aspects

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 25))

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.(Mol Cell Biochem 184:: 141–151, 1998)

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Stachowiak, O., Schlattner, U., Dolder, M., Wallimann, T. (1998). Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: Implications for cellular function and mitochondrial structure. In: Saks, V.A., Ventura-Clapier, R., Leverve, X., Rossi, A., Rigoulet, M. (eds) Bioenergetics of the Cell: Quantitative Aspects. Developments in Molecular and Cellular Biochemistry, vol 25. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5653-4_11

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