[KRP/telokin differentially regulates filament assembly and phosphorylation of light chains of non-muscle myosin II in fibroblasts].
Transgenic 3T3 fibroblasts have been generated that express either the wild-type KRP or its truncated mutant lacking the C-terminal domain, which primarily contributes to myosin binding of KRP. It was found that KRP-expressing cells display a significantly increased content of myosin filaments and a reduced level of rMLC phosphorylation, whereas the mock transfected cells or cells expressing the C-terminally truncated KRP do not. Our results suggest that (1) KRP promotes the polymerization of myosin II and reduces the rMLC phosphorylation level in cells, (2) KRP acts through direct binding to myosin II, and (3) transgenic 3T3 fibroblasts stably expressing KRP represent a useful and versatile model to study the role of myosin II filament dynamics in cell motility.
Serebrianaia
D B
DB
Shcherbakova
O V
OV
Dudnakova
T V
TV
Shirinskiĭ
V P
VP
Vorotnikov
A V
AV
D008841:Actin Cytoskeleton / Q000378:metabolism*; D000818:Animals; D001704:Biopolymers; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000502:physiology*; D005347:Fibroblasts / Q000378:metabolism*; D051379:Mice; D018994:Myosin Light Chains / Q000378:metabolism*; D024462:Myosin Type II / Q000378:metabolism*; D009219:Myosin-Light-Chain Kinase / Q000235:genetics / Q000502:physiology*; D041681:NIH 3T3 Cells; D010766:Phosphorylation; D019076:Transgenes
D001704:Biopolymers; D002135:Calcium-Binding Proteins; D018994:Myosin Light Chains; C499378:MYLK protein, human; D009219:Myosin-Light-Chain Kinase; D024462:Myosin Type II