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- W566904215 abstract "Previous work has suggested that in addition to its kinase activity, myosin light chain kinase exhibits non-kinase properties that could influence cytoskeletal organization. Colocalization imaging and fluorescence resonance energy transfer (FRET) analysis indicated α-actin/MLCK association in resting cells and in podosomes of phorbol 12,13dibutyrate (PDBu)-stimulated A7r5 smooth muscle cells. By comparison, β-actin/MLCK association was observed in stress fibers and in diffuse distribution in the perinuclear region of both control and PDBu-treated cells. Downregulation of MLCK by siRNA transfection resulted in variable patterns of actin isoform reorganization in control cells. α-Actin formed a dense system of filaments at the cell periphery leaving the central region of the cells devoid of structure. In contrast, β-actin stress fibers disassembled with this isoform diffusely distributed in the cell. In PDBu-treated cells, transfection with MLCK-siRNA resulted in an approximate 70% reduction in the formation of podosomes. The introduction of a peptide containing the 1-41 N-terminal amino acid sequence of MLCK by peptide-mediated uptake or microinjection resulted in loss of α-actin stress fibers from the central region of the cell. The results indicate that MLCK plays an important role in maintaining αand β-actin stress fibers and in the phorbol ester-induced reorganization of these isoforms. Furthermore, this role appears to be related to the Nterminal actin binding properties of the kinase." @default.
- W566904215 created "2016-06-24" @default.
- W566904215 creator A5048488685 @default.
- W566904215 date "2007-01-01" @default.
- W566904215 modified "2023-09-27" @default.
- W566904215 title "MLCK/actin Interaction in the Contracting A7r5 Cell and Vascular Smooth Muscle" @default.
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