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| Item Type: | Article |
|---|---|
| Title: | Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein |
| Creators Name: | Hornemann, T., Kempa, S., Himmel, M., Hayess, K., Fuerst, D.O. and Wallimann, T. |
| Abstract: | Muscle-type creatine kinase (MM-CK) is a member of the CK isoenzyme family with key functions in cellular energetics. MM-CK interacts in an isoform-specific manner with the M-band of sarcomeric muscle, where it serves as an efficient intramyofibrillar ATP-regenerating system for the actin-activated myosin ATPase located nearby on both sides of the M-band. Four MM-CK-specific and highly conserved lysine residues are thought to be responsible for the interaction of MM-CK with the M-band. A yeast two-hybrid screen led to the identification of MM-CK as a binding partner of a central portion of myomesin (My7-8). An interaction was observed with domains six to eight of the closely related M-protein but not with several other Ig-like domains, including an M-band domain, of titin. The observed interactions were corroborated and characterised in detail by surface plasmon resonance spectroscopy (BiaCore). In both cases, they were CK isoform-specific and the MM-CK-specific lysine residues (K8. K24, K104 and K115) are involved in this interaction. At pH 6.8, the dissociation constants for the myomesin/MM-CK and the M-protein/MM-CK binding were in the range of 50-100 nM and around 1 microM, respectively. The binding showed pronounced pH-dependence and indicates a dynamic association/dissociation behaviour, which most likely depends on the energy state of the muscle. Our data propose a simple model for the regulation of this dynamic interaction. |
| Keywords: | Creatine Kinase, Myomesin, M-Protein, Sarcomeric M-Band, Titin, Animals, Chickens |
| Source: | Journal of Molecular Biology |
| ISSN: | 0022-2836 |
| Publisher: | Academic Press |
| Volume: | 332 |
| Number: | 4 |
| Page Range: | 877-887 |
| Date: | 26 September 2003 |
| Official Publication: | https://doi.org/10.1016/S0022-2836(03)00921-5 |
| PubMed: | View item in PubMed |
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