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

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 f...

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Bibliographic Details
Published inMolecular and cellular biochemistry Vol. 184; no. 1-2; pp. 141 - 151
Main Authors Stachowiak, O, Schlattner, U, Dolder, M, Wallimann, T
Format Journal Article
LanguageEnglish
Published Netherlands Springer Nature B.V 01.07.1998
Springer Verlag
Subjects
Binding Sites - physiology
Cell Membrane - metabolism
Cellular biology
Creatine Kinase - chemistry
Isoenzymes
Kinases
Kinetics
Life Sciences
Membranes
Mitochondria
Mitochondria - enzymology
Mitochondria - physiology
Models, Molecular
Protein Binding - physiology
Protein Conformation
lipid vesicle cross-linking
VDAC (porin)
dimer/octamer equilibrium
Mi-CK
membrane binding domains
ANT
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1006803431821