| First Author | Nixon BR | Year | 2013 |
| Journal | Arch Biochem Biophys | Volume | 535 |
| Issue | 1 | Pages | 30-8 |
| PubMed ID | 23232082 | Mgi Jnum | J:205612 |
| Mgi Id | MGI:5545933 | Doi | 10.1016/j.abb.2012.11.010 |
| Citation | Nixon BR, et al. (2013) Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation. Arch Biochem Biophys 535(1):30-8 |
| abstractText | Tropomyosin (Tm) is a central protein in the Ca(2+) regulation of striated muscle. The alphaTm isoform undergoes phosphorylation at serine residue 283. While the biochemical and steady-state muscle function of muscle purified Tm phosphorylation have been explored, the effects of Tm phosphorylation on the dynamic properties of muscle contraction and relaxation are unknown. To investigate the kinetic regulatory role of alphaTm phosphorylation we expressed and purified native N-terminal acetylated Ser-283 wild-type, S283A phosphorylation null and S283D pseudo-phosphorylation Tm mutants in insect cells. Purified Tm's regulate thin filaments similar to that reported for muscle purified Tm. Steady-state Ca(2+) binding to troponin C (TnC) in reconstituted thin filaments did not differ between the 3 Tm's, however disassociation of Ca(2+) from filaments containing pseudo-phosphorylated Tm was slowed compared to wild-type Tm. Replacement of pseudo-phosphorylated Tm into myofibrils similarly prolonged the slow phase of relaxation and decreased the rate of the fast phase without altering activation kinetics. These data demonstrate that Tm pseudo-phosphorylation slows deactivation of the thin filament and muscle force relaxation dynamics in the absence of dynamic and steady-state effects on muscle activation. This supports a role for Tm as a key protein in the regulation of muscle relaxation dynamics. |
