A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces actin cytoskeletal reorganization

Kazumasa Ohashi, Toshihiko Hosoya, Kazuya Takahashi, Huey Hing, Kensaku Mizuno

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50 Citations (Scopus)


Mammalian LIM-kinases (LIMKs) phosphorylate cofilin and induce actin cytoskeletal reorganization. To elucidate the functional roles of LIMKs in vivo during developmental processes, we attempted to isolate the cDNA encoding a Drosophila homolog of LIMK (DLIMK) and identified two isoforms of DLIMK transcripts coding for proteins with 1235 and 1257 amino acids, possessing the structure composed of two LIM domains, a PDZ domain, a protein kinase domain, and an unusual long C-terminal extension. In situ hybridization analysis in Drosophila embryos detected the uniformly distributed DLIMK mRNA in stages 2 to 5. In vitro kinase reaction revealed that DLIMK efficiently phosphorylates Drosophila cofilin (twinstar) specifically at Ser-3, the site responsible for inactivation of its actin-depolymerizing activity. When expressed in cultured cells, wild-type DLIMK, but not its kinase-inactive form, induced changes in actin cytoskeletal organization. These observations suggest that the LIMK-cofilin signaling pathway for regulating actin filament dynamics is evolutionarily conserved between Drosophila and mammals. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1178-1185
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 2000 Oct 5


  • Actin reorganization
  • Cofilin
  • Drosophila
  • In situ hybridization
  • LIM-kinase
  • Twinstar


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