FEBS Letters | |
Differential localization of non‐muscle myosin II isoforms and phosphorylated regulatory light chains in human MRC‐5 fibroblasts | |
Takemura, Shuhei3  Kawabata, Kazushige4  Saitoh, Takayuki3  Yamagishi, Akihiko3  Haga, Hisashi4  Hosoya, Hiroshi2  Nagayama, Masafumi4  Takahashi, Masayuki1  Ueda, Kozue2  | |
[1] Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan;Department of Biological Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan;Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan;Division of Physics, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan | |
关键词: Myosin II heavy chain isoform; Regulatory light chain; Phosphorylation; Localization; Cell migration; Stress fiber; | |
DOI : 10.1016/S0014-5793(01)03186-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We investigated the localization of non-muscle myosin II isoforms and mono- (at serine 19) and diphosphorylated (at serine 19 and threonine 18) regulatory light chains (RLCs) in motile and non-motile MRC-5 fibroblasts. In migrating cells, myosin IIA localized to the lamella and throughout the posterior region. Myosin IIB colocalized with myosin IIA to the posterior region except at the very end. Diphosphorylated RLCs were detected in the restricted region where myosin IIA was enriched. In non-motile cells, myosin IIA was enriched in peripheral stress fibers with diphosphorylated RLCs, but myosin IIB was not. Our results suggest that myosin IIA may be highly activated by diphosphorylation of RLCs and primarily involved in cell migration.
【 授权许可】
Unknown
【 预 览 】
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