%0 Journal Article %1 John_1996_761 %A Johnson, J. D. %A Snyder, C. %A Walsh, M. %A Flynn, M. %D 1996 %J J. Biol. Chem. %K 8557684 Acid Amino Animals, Binding Calcium, Calmodulin, Cattle, Computer Data, Dependent Gov't, Kinase, Molecular Myosin-Light-Chain Non-U.S. P.H.S., Protein Research Sequence Sequence, Simulation, Sites, Support, U.S. {C}a$^{2+}$-Calmodulin %N 2 %P 761--767 %T Effects of myosin light chain kinase and peptides on Ca$^2+$ exchange with the N- and C-terminal Ca$^2+$ binding sites of calmodulin. %U http://www.jbc.org/cgi/content/full/271/2/761 %V 271 %X Myosin light chain kinase and peptides from the calmodulin (CaM) binding domains of myosin light chain kinase (RS-20, M-13), CaM kinase II, and the myristoylated alanine-rich protein kinase C substrate protein slowed Ca$^2+$ dissociation from CaM's N-terminal sites from 405 +/- 75/s to 1.8-2.9/s and from CaM's C-terminal sites from 2.4 +/- 0.2/s to 0.1-0.4/s at 10 degrees C. Since Ca$^2+$ dissociates 5-29 times faster from the N-terminal in these CaM.peptide complexes and both lobes are required for activation, Ca$^2+$ dissociation from the N-terminal would control target protein inactivation. Ca$^2+$ binds 70 times faster to the N-terminal (1.6 x 10(8) M-1 s-1) than the C-terminal sites (2.3 x 10(6) M-1 s-1). In a 0.6-ms half-width Ca$^2+$ transient, Ca$^2+$ occupied > 70\% of the N-terminal but only 20\% of the C-terminal sites. RS-20 produced a 9-fold and CaM kinase II a 6.3-fold increase in C-terminal Ca$^2+$ affinity, suggesting that some target proteins may be bound to the C-terminal at resting Ca$^2+$. When this is the case, Ca$^2+$ exchange with the faster N-terminal sites may regulate CaM's activation and inactivation of these target proteins during a Ca$^2+$ transient.

@article{John_1996_761, abstract = {Myosin light chain kinase and peptides from the calmodulin (CaM) binding domains of myosin light chain kinase (RS-20, M-13), CaM kinase II, and the myristoylated alanine-rich protein kinase C substrate protein slowed {C}a$^{2+}$ dissociation from CaM's N-terminal sites from 405 +/- 75/s to 1.8-2.9/s and from CaM's C-terminal sites from 2.4 +/- 0.2/s to 0.1-0.4/s at 10 degrees C. Since {C}a$^{2+}$ dissociates 5-29 times faster from the N-terminal in these CaM.peptide complexes and both lobes are required for activation, {C}a$^{2+}$ dissociation from the N-terminal would control target protein inactivation. {C}a$^{2+}$ binds 70 times faster to the N-terminal (1.6 x 10(8) M-1 s-1) than the C-terminal sites (2.3 x 10(6) M-1 s-1). In a 0.6-ms half-width {C}a$^{2+}$ transient, {C}a$^{2+}$ occupied > 70\% of the N-terminal but only 20\% of the C-terminal sites. RS-20 produced a 9-fold and CaM kinase II a 6.3-fold increase in C-terminal {C}a$^{2+}$ affinity, suggesting that some target proteins may be bound to the C-terminal at resting [{C}a$^{2+}$]. When this is the case, {C}a$^{2+}$ exchange with the faster N-terminal sites may regulate CaM's activation and inactivation of these target proteins during a {C}a$^{2+}$ transient.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Johnson, J. D. and Snyder, C. and Walsh, M. and Flynn, M.}, biburl = {https://www.bibsonomy.org/bibtex/25ae690cd051c44768b18b8633a0d84c5/hake}, description = {The whole bibliography file I use.}, file = {John_1996_761.pdf:John_1996_761.pdf:PDF}, interhash = {ddc728f5b135cf6d91af7fe26e9c1a3f}, intrahash = {5ae690cd051c44768b18b8633a0d84c5}, journal = {J. Biol. Chem.}, keywords = {8557684 Acid Amino Animals, Binding Calcium, Calmodulin, Cattle, Computer Data, Dependent Gov't, Kinase, Molecular Myosin-Light-Chain Non-U.S. P.H.S., Protein Research Sequence Sequence, Simulation, Sites, Support, U.S. {C}a$^{2+}$-Calmodulin}, month = Jan, number = 2, pages = {761--767}, pmid = {8557684}, timestamp = {2009-06-03T11:21:17.000+0200}, title = {Effects of myosin light chain kinase and peptides on {C}a$^{2+}$ exchange with the N- and C-terminal {C}a$^{2+}$ binding sites of calmodulin.}, url = {http://www.jbc.org/cgi/content/full/271/2/761}, volume = 271, year = 1996 }