1998
DOI: 10.1074/jbc.273.36.22990
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Octamer Formation and Coupling of Cardiac Sarcomeric Mitochondrial Creatine Kinase Are Mediated by Charged N-terminal Residues

Abstract: Mitochondrial creatine kinases form octameric structures composed of four active and stable dimers. Octamer formation has been postulated to occur via interaction of the charged amino acids in the N-terminal peptide of the mature enzyme. We altered codons for charged amino acids in the N-terminal region of mature sarcomeric mitochondrial creatine kinase (sMtCK) to those encoding neutral amino acids. Transfection of normal sMtCK cDNA or those with the mutations R42G, E43G/H45G, and K46G into rat neonatal cardio… Show more

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Cited by 63 publications
(57 citation statements)
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“…topology could accommodate interaction with four ANT dimers, giving rise to a molar dimer ratio of about 1:1 in such a proteolipid complex as already speculated earlier (56). The CL interactions of MtCK, together with its octameric structure, are important prerequisites for the formation of the functional microcompartments with ANT (3,30). These microcompartments control metabolite channeling between CK and ANT (Fig.…”
Section: Discussionmentioning
confidence: 86%
See 1 more Smart Citation
“…topology could accommodate interaction with four ANT dimers, giving rise to a molar dimer ratio of about 1:1 in such a proteolipid complex as already speculated earlier (56). The CL interactions of MtCK, together with its octameric structure, are important prerequisites for the formation of the functional microcompartments with ANT (3,30). These microcompartments control metabolite channeling between CK and ANT (Fig.…”
Section: Discussionmentioning
confidence: 86%
“…It may allow for close co-localization of MtCK and ANT in proteolipid complexes, possibly through CL membrane patches. In support of this, mutations that reduce MtCK membrane binding through destabilization of its octameric structure also reduce creatinestimulated respiration in cardiomyocyte mitochondria (30). In fact, it is well known that CL-protein interactions are important not only for activity and structural integrity of mitochondrial inner membrane proteins but also for subunit assembly and supercomplex formation (31)(32)(33)(34).…”
mentioning
confidence: 99%
“…12,14,15 Furthermore, there is strong evidence that metabolic impairment and mitochondrial dysfunction are involved in the pathophysiology of BD. [16][17][18][19][20] The phosphocreatine/ CK energy circuit, which is important for maintaining normal energy homeostasis, 21,22 has a number of integrated functions, such as temporary energy buffering and energy transfer, as well as regulating metabolic capacity. 23 In view of these data, we can suggest that the increased CK activity seen in manic BD patients is a compensatory mechanism related to the mitochondrial damage that occurs in BD.…”
Section: Discussionmentioning
confidence: 99%
“…In contrast to dimeric cytosolic CK isoenzymes, mitochondrial isoenzymes occur as two interconvertible oligomeric species, dimers and octamers (38). The latter is predominant in vivo and is considered as the physiologically active species that binds to mitochondrial membranes and functions in cellular energy transduction (23). In both control and DXR-treated samples, sMtCK dimers were hardly detectable in CPAE performed under standard conditions (Figs.…”
Section: Dxr Impairs Myocardial Function In a Dose-dependent Mannermentioning
confidence: 99%