Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L |
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Authors: | Yamamoto Masahiro Nagata-Ohashi Kyoko Ohta Yusaku Ohashi Kazumasa Mizuno Kensaku |
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Affiliation: | Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan. |
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Abstract: | 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. |
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Keywords: | FL, full-length P-cofilin, Ser-3-phosphorylated cofilin SSH, Slingshot SSH1L, a long form of Slingshot-1 WT, wild-type |
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