Myosin-Light-Chain Kinase

• 

  Subject Areas on Research

  • Acceleration of myosin light chain dephosphorylation and relaxation of smooth muscle by telokin. Synergism with cyclic nucleotide-activated kinase. 
  • Activation of four enzymes by two series of calmodulin mutants with point mutations in individual Ca2+ binding sites. 
  • Association of calmodulin and smooth muscle myosin light chain kinase: application of a label selection technique with trace acetylated calmodulin. 
  • Association of myosin light chain kinase with lymphocyte membrane-cytoskeleton complex. 
  • Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase. 
  • Calcium dynamics underlying the myogenic response of the renal afferent arteriole. 
  • Calcium/calmodulin transduces thrombin-stimulated secretion: studies in intact and minimally permeabilized human umbilical vein endothelial cells. 
  • Calmodulin activation of target enzymes. Consequences of deletions in the central helix. 
  • Calmodulin in endocrine cells. 
  • Calmodulin kinase II chimeras used to investigate the structural requirements for smooth muscle myosin light chain kinase autoinhibition and calmodulin-dependent activation. 
  • Calmodulin regulation of smooth-muscle myosin light-chain kinase. 
  • Calmodulin-cardiac troponin C chimeras. Effects of domain exchange on calcium binding and enzyme activation. 
  • Calmodulin-myosin light chain kinase inhibition changes fibroblast-populated collagen lattice contraction, cell migration, focal adhesion formation, and wound contraction. 
  • Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase. 
  • Characterization and analysis of an apparent autophosphorylation of chicken gizzard myosin light chain kinase. 
  • Characterization of cytoskeleton-enriched protein fraction of the trabecular meshwork and ciliary muscle cells. 
  • Characterization of the secondary structure of calmodulin in complex with a calmodulin-binding domain peptide. 
  • Chimeric calmodulin-cardiac troponin C proteins differentially activate calmodulin target enzymes. 
  • Cytokinesis. 
  • Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. 
  • Drosophila stretchin-MLCK is a novel member of the Titin/Myosin light chain kinase family. 
  • Estrogen stimulates the transient association of calmodulin and myosin light chain kinase with the chicken liver nuclear matrix. 
  • Fluorescence linked enzyme chemoproteomic strategy for discovery of a potent and selective DAPK1 and ZIPK inhibitor. 
  • Function and regulation of calmodulin in endocrine cells. 
  • Functional consequences of truncating amino acid side chains located at a calmodulin-peptide interface. 
  • Functional domains of chicken gizzard myosin light chain kinase. 
  • Functional significance of the central helix in calmodulin. 
  • Genetically engineered calmodulins differentially activate target enzymes. 
  • Hormonal regulation of a chicken oviduct messenger ribonucleic acid that shares a common domain with gizzard myosin light chain kinase. 
  • Identification of amino acids essential for calmodulin binding and activation of smooth muscle myosin light chain kinase. 
  • Intrasteric regulation of myosin light chain kinase: the pseudosubstrate prototope binds to the active site. 
  • Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases. 
  • Molecular analysis of calmodulin and smooth muscle myosin light chain kinase. 
  • Myosin light chain kinase structure function analysis using bacterial expression. 
  • Ontogenesis of myosin light chain kinase mRNA and protein content in guinea pig tracheal smooth muscle. 
  • Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. 
  • Phosphorylation-dependent power output of transgenic flies: an integrated study. 
  • Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. 
  • Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-independent fragments. 
  • Quantitation and significance of 125I-calmodulin binding to myosin light chain kinase and phosphorylase distributed on polyacrylamide gels. 
  • ROCK1 phosphorylates and activates zipper-interacting protein kinase. 
  • Regulation of protein kinases by pseudosubstrate prototopes. 
  • Regulation of smooth muscle myosin light chain kinase by calmodulin. 
  • Regulatory and structural motifs of chicken gizzard myosin light chain kinase. 
  • Regulatory cascades involving calmodulin-dependent protein kinases. 
  • Regulatory functions of calmodulin. 
  • Role of autophosphorylation in regulating calmodulin-dependent protein kinases. 
  • Secondary heart field contributes myocardium and smooth muscle to the arterial pole of the developing heart. 
  • Selective activation and inhibition of calmodulin-dependent enzymes by a calmodulin-like protein found in human epithelial cells. 
  • Site-specific phosphorylation and point mutations of telokin modulate its Ca2+-desensitizing effect in smooth muscle. 
  • Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy. 
  • Structural basis of the intrasteric regulation of myosin light chain kinases. 
  • Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin. 
  • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. 
  • The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. 
  • Three amino acid substitutions in domain I of calmodulin prevent the activation of chicken smooth muscle myosin light chain kinase. 
  • Three paradigms of airway smooth muscle hyperresponsiveness in young guinea pigs. 
  • Use of the 125I-labeled protein gel overlay technique to study calmodulin-binding proteins. 
• 

  Keywords of People

  • Erickson, Harold Paul, James B. Duke Professor of Cell Biology, Biomedical Engineering