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Identification of multiple actin‐binding sites in cofilin‐phosphatase Slingshot‐1L
Author(s) -
Yamamoto Masahiro,
Nagata-Ohashi Kyoko,
Ohta Yusaku,
Ohashi Kazumasa,
Mizuno Kensaku
Publication year - 2006
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/j.febslet.2006.02.034
Subject(s) - cofilin , phosphatase , actin , subcellular localization , microbiology and biotechnology , actin binding protein , chemistry , actin remodeling , biochemistry , actin cytoskeleton , biology , cytoskeleton , phosphorylation , cytoplasm , cell
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.