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Differential localization of non‐muscle myosin II isoforms and phosphorylated regulatory light chains in human MRC‐5 fibroblasts
Author(s) -
Saitoh Takayuki,
Takemura Shuhei,
Ueda Kozue,
Hosoya Hiroshi,
Nagayama Masafumi,
Haga Hisashi,
Kawabata Kazushige,
Yamagishi Akihiko,
Takahashi Masayuki
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03186-6
Subject(s) - myosin , serine , gene isoform , myosin light chain kinase , phosphorylation , myosin head , biology , myh7 , actin , microbiology and biotechnology , biochemistry , gene
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.