Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L

Masahiro Yamamoto, Kyoko Nagata-Ohashi, Yusaku Ohta, Kazumasa Ohashi, Kensaku Mizuno

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


Slingshot-1L (SSH1L) is a phosphatase that specifically dephosphorylates and activates cofilin, an actin-severing and -depolymerizing protein. SSH1L binds to and is activated by F-actin in vitro, and co-localizes with F-actin in cultured cells. We examined the F-actin-binding activity, F-actin-mediated phosphatase activation, and subcellular distribution of various mutants of SSH1L. We identified three sites involved in F-actin binding of SSH1L: Trp-458 close to the C-terminus of the phosphatase domain, an LHK motif in the N-terminal region, and an LKR motif in the C-terminal region. These sites play unique roles in the control of subcellular localization and F-actin-mediated activation of SSH1L.

Original languageEnglish
Pages (from-to)1789-1794
Number of pages6
JournalFEBS Letters
Issue number7
Publication statusPublished - 2006 Mar 20


  • Actin-binding
  • Cofilin
  • Phosphatase
  • Slingshot

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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