Identification of multiple actin‐binding sites in cofilin‐phosphatase Slingshot‐1L
Identification of multiple actin‐binding sites in cofilin‐phosphatase Slingshot‐1L
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DOI：
10.1016/j.febslet.2006.02.034
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发表时间：
2006-03
期刊：
影响因子：
3.5
通讯作者：
Masahiro Yamamoto;Kyoko Nagata-Ohashi;Yusaku Ohta;K. Ohashi;K. Mizuno
中科院分区：
文献类型：
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作者：
Masahiro Yamamoto;Kyoko Nagata-Ohashi;Yusaku Ohta;K. Ohashi;K. Mizuno
Slingshot-1 L（SSH 1 L）是一种磷酸酶，其特异性地去磷酸化并激活cofilin，一种肌动蛋白切断和解聚蛋白。SSH 1 L在体外与F-肌动蛋白结合并被其激活，并在培养的细胞中与F-肌动蛋白共定位。我们研究了F-肌动蛋白结合活性，F-肌动蛋白介导的磷酸酶激活，和SSH 1 L的各种突变体的亚细胞分布。我们确定了三个参与SSH 1 L的F-肌动蛋白结合的位点：靠近磷酸酶结构域C-末端的Trp-458，N-末端区域的LHK基序和C-末端区域的LKR基序。这些位点在控制SSH 1 L的亚细胞定位和F-肌动蛋白介导的激活中发挥独特的作用。
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.