Blumenthal D K, Charbonneau H, Edelman A M, Hinds T R, Rosenberg G B, Storm D R, Vincenzi F F, Beavo J A, Krebs E G
Howard Hughes Medical Institute, University of Washington, Seattle 98195.
Biochem Biophys Res Commun. 1988 Oct 31;156(2):860-5. doi: 10.1016/s0006-291x(88)80923-9.
Nanomolar concentrations of synthetic peptides corresponding to the calmodulin-binding domain of skeletal muscle myosin light chain kinase were found to inhibit calmodulin activation of seven well-characterized calmodulin-dependent enzymes: brain 61 kDa cyclic nucleotide phosphodiesterase, brain adenylate cyclase, Bordetella pertussis adenylate cyclase, red blood cell membrane Ca++-pump ATPase, brain calmodulin-dependent protein phosphatase (calcineurin), skeletal muscle phosphorylase b kinase, and brain multifunctional Ca++ (calmodulin)-dependent protein kinase. Inhibition could be entirely overcome by the addition of excess calmodulin. Thus, the myosin light chain kinase peptides used in this study may be useful antagonists for studying calmodulin-dependent enzymes and processes.
