Distinct roles of four gelsolin-like domains of Caenorhabditis elegans gelsolin-like protein-1 in actin filament severing, barbed end capping, and phosphoinositide binding.
Distinct roles of four gelsolin-like domains of Caenorhabditis elegans gelsolin-like protein-1 in actin filament severing, barbed end capping, and phosphoinositide binding.
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DOI：
10.1021/bi100215b
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发表时间：
2010-05-25
期刊：
影响因子：
2.9
通讯作者：
Ono, Shoichiro
中科院分区：
文献类型：
--
作者：
Liu, Zhongmei;Klaavuniemi, Tuula;Ono, Shoichiro
它是一种非常规的凝溶胶蛋白相关蛋白，具有四个凝溶胶蛋白样（G）结构域（G1至G4），不同于典型的凝溶胶蛋白相关蛋白具有三个或六个G结构域。GSNL-1切断肌动蛋白丝，并以类似于凝溶胶蛋白的钙依赖性方式覆盖倒刺末端。相比之下，GSNL-1具有与凝溶胶蛋白不同的性质，因为它保持与F-肌动蛋白结合，并且不使肌动蛋白聚合成核。为了理解GSNL-1调节肌动蛋白动力学的机制，我们通过分析截短形式的GSNL-1的活性来研究GSNL-1的结构域-功能关系。G1加上G1和G2之间的连接子足以切断肌动蛋白丝，而G1和G2则需要倒钩末端加帽。GSNL-1的肌动蛋白切割活性被磷脂酰肌醇4，5-二磷酸（PIP 2）抑制，并且PIP 2敏感结构域被定位到G1-G2。检测到至少两个肌动蛋白结合位点：G1中的钙依赖性G-肌动蛋白结合位点和G3-G4中的钙非依赖性G-和F-肌动蛋白结合位点。这些结果揭示了C.线虫GSNL-1和哺乳动物凝溶胶蛋白的肌动蛋白调节功能。
It is an unconventional gelsolin-related protein with four gelsolin-like (G) domains (G1 to G4), unlike typical gelsolin-related proteins with three or six G domains. GSNL-1 severs actin filaments and caps the barbed end in a calcium-dependent manner similarly to gelsolin. In contrast, GSNL-1 has different properties from gelsolin in that it remains bound to F-actin, and does not nucleate actin polymerization. To understand the mechanism by which GSNL-1 regulates actin dynamics, we investigated domain-function relationship of GSNL-1 by analyzing activities of truncated forms of GSNL-1. G1 plus the linker between G1 and G2 was sufficient for actin filament severing, whereas G1 and G2 were required for barbed-end capping. Actin severing activity of GSNL-1 was inhibited by phosphatidylinositol 4,5-bisphosphate (PIP2), and a PIP2-sensitive domain was mapped to G1–G2. At least two actin-binding sites were detected: a calcium-dependent G-actin-binding site in G1 and a calcium-independent G- and F-actin-binding site in G3–G4. These results reveal both conserved and different utilization of G domains between C. elegans GSNL-1 and mammalian gelsolin for actin-regulatory functions.
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