Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates

Autor: Josh E. Baker, Brian D. Haldeman, Diego B. Alcala, Agata K. Krenc, Christine R. Cremo, Richard K. Brizendine, Ronald S. Rock

Publikováno v: Cell Biochemistry and Function. 34:469-474

Myosin light chain kinase (MLCK) phosphorylates S19 of the myosin regulatory light chain (RLC), which is required to activate myosin's ATPase activity and contraction. Smooth muscles are known to display plasticity in response to factors such as infl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::035822c97970b26685b80debc5717f17
https://doi.org/10.1002/cbf.3209

Kinetics of Myosin Light Chain Kinase Activation of Smooth Muscle Myosin in an in Vitro Model System

Autor: Michael S. Carter, Christine R. Cremo, Nick Ruana, Brian D. Haldeman, Cindy Sutherland, Feng Hong, Del R. Jackson, Michael P. Walsh, Josh E. Baker, Kevin C. Facemyer

Publikováno v: Biochemistry. 52:8489-8500

When activated by Ca2+CaM, MLCK phosphorylates the SMM RLC at Ser19, which activates the actin-SMM ATPase leading to the cyclic interactions of SMM with actin required for smooth muscle contraction.1-3 In smooth muscle, MLCK is in low abundance relat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb1d3665f5ca8cb952b8802007102104
https://doi.org/10.1021/bi401001x

Modification of Interface between Regulatory and Essential Light Chains Hampers Phosphorylation-dependent Activation of Smooth Muscle Myosin

Autor: Josh E. Baker, Shaowei Ni, Christine R. Cremo, Brian D. Haldeman, Feng Hong, Kevin C. Facemyer

Publikováno v: Journal of Biological Chemistry. 287:22068-22079

We examined the regulatory importance of interactions between regulatory light chain (RLC), essential light chain (ELC), and adjacent heavy chain (HC) in the regulatory domain of smooth muscle heavy meromyosin. After mutating the HC, RLC, and/or ELC

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33cf744ca04d6e0d0eda32b4fdac7b0d
https://doi.org/10.1074/jbc.m112.343491

Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation

Autor: Jean Chamoun, Likai Song, Paul J. Brewer, Christine R. Cremo, Piotr G. Fajer, Brian D. Haldeman, Bridget Salzameda, Hua Liang, Hui-Chun Li, Kevin C. Facemyer, Bertrand Vileno

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (20), pp.8218-8223. ⟨10.1073/pnas.1014137108⟩

Double electron electron resonance EPR methods was used to measure the effects of the allosteric modulators, phosphorylation, and ATP, on the distances and distance distributions between the two regulatory light chain of myosin (RLC). Three different

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d16b36a990a06e3ae1150067228401f
https://doi.org/10.1073/pnas.1014137108

Varying the Number of Heads in Phosphorylated Smooth Muscle Myosin Filaments Provides Evidence for Attachment Limited Kinetics of in vitro Actin-Sliding Velocities

Autor: Diego B. Alcala, Richard K. Brizendine, Christine R. Cremo, Brian D. Haldeman, Josh E. Baker, Kevin C. Facemyer

Publikováno v: Biophysical Journal. 108:296a-297a

Previously we have shown that the ATP-dependence of EDC-stabilized fluorescent smooth muscle myosin (SMM) filament motility is very similar to solution ATPase values (KATP = 8.5 and 9.2 µM, respectively). This suggests both processes are influenced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53c3bf1e340f510dad70149c855b3f17
https://doi.org/10.1016/j.bpj.2014.11.1613