Filamentous smooth muscle myosin is regulated by phosphorylation

  title={Filamentous smooth muscle myosin is regulated by phosphorylation},
  author={Kathleen M Trybus},
  journal={The Journal of Cell Biology},
  pages={2887 - 2894}
The enzymatic activity of filamentous dephosphorylated smooth muscle myosin has been difficult to determine because the polymer disassembles to the folded conformation in the presence of MgATP. Monoclonal antirod antibodies were used here to "fix" dephosphorylated myosin in the filamentous state. The steady-state actin-activated ATPase of phosphorylated filaments was 30-100-fold higher than that of antibody-stabilized dephosphorylated filaments, suggesting that phosphorylation can activate… CONTINUE READING
Highly Cited
This paper has 35 citations. REVIEW CITATIONS


Publications citing this paper.
Showing 1-10 of 24 extracted citations


Publications referenced by this paper.
Showing 1-10 of 32 references

Analysis of the birefringence of the smooth muscle anococcygeus of the rat, at rest and in contraction

  • A. Godfraind-DeBecker, J. M. Gillis.
  • I. J. Muscle Res. Cell Motil. 9:9-17.
  • 1988
1 Excerpt