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首页> 外文期刊>Cell motility and the cytoskeleton >Hair-forming activity of human lymphocyte specific protein 1 requires cooperation between its caldesmon-like domains and the villin headpiece-like domains.
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Hair-forming activity of human lymphocyte specific protein 1 requires cooperation between its caldesmon-like domains and the villin headpiece-like domains.

机译：人淋巴细胞特异性蛋白1的头发形成活性需要其caldesmon样结构域和villin头饰样结构域之间的协作。

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摘要

LSP1 is an F-actin binding with multiple F-actin binding domains. Overexpression of LSP1 in NAD 47/89 patient's neutrophils created hair-like projections on the patient's neutrophil cell surfaces and inhibited neutrophil cell motility and transfection of LSP1 in serial cell lines recreate the NAD 47/89 phenotype and produce branching hair-like surface projections. Although LSP1 contains hair-forming ability and LSP1 F-actin binding domains have been defined, the LSP1 domains responsible for its hair-forming activity, the relationship to the F-actin binding domains, and the required domain interactions, if any, for hair formation are not well understood. To define the hair-forming domains of LSP1, the relationship to the known F-actin binding domains, and binding domain interactions, LSP1 truncates, which include or exclude the different F-actin binding domains, were created by PCR. LSP1 mutants were created by site-directed mutagenesis to define the amino acids important for hair formation. Sf9 cells were infected with recombinant baculovirus expressing the cDNA of LSP1 truncates and mutants, and the morphology of infected Sf9 cells was documented by DIC optics. Results show that (1) the hair-forming activity of LSP1 is localized to the basic C-terminal half of the molecule, which contains all of the F-actin binding domains; (2) both the caldesmon-like domains and the villin headpiece-like domains are required for the hair-forming activity of LSP1; (3) basic amino acids in the villin headpiece regions are crucial for the hair-forming activity of LSP1 molecule. The results suggest cooperation between the caldesmon-like domains and the villin headpiece-like domains are required for the hair-forming activity of human LSP1 in cells. Copyright 2001 Wiley-Liss, Inc.
机译：LSP1是具有多个F-肌动蛋白结合域的F-肌动蛋白结合。 LSP1在NAD 47/89患者的中性粒细胞中的过表达在患者的中性粒细胞表面上形成了毛状突起，并抑制了中性粒细胞的活力，LSP1在连续细胞系中的转染重建了NAD 47/89表型并产生了分支状的毛状表面突起。尽管LSP1具有毛发形成能力，并且已经定义了LSP1 F-肌动蛋白结合域，但是负责其毛发形成活动，与F-actin结合域的关系以及所需的毛发域交互作用的LSP1域形成尚不清楚。为了定义LSP1的毛发形成域，通过PCR创建了与已知F-肌动蛋白结合域的关系以及结合域的相互作用，LSP1截短了包括或排除了不同的F-肌动蛋白结合域。通过定点诱变创建LSP1突变体，以定义对头发形成重要的氨基酸。用表达LSP1截短和突变体cDNA的重组杆状病毒感染Sf9细胞，并通过DIC光学仪器记录感染的Sf9细胞的形态。结果表明：（1）LSP1的生发活性位于分子的基本C末端一半，其中包含所有F-肌动蛋白结合域; （2）LSP1的毛发形成过程既需要caldesmon样结构域，也需要使用villin headpiece样结构域。 （3）villin头饰区的碱性氨基酸对于LSP1分子的毛发形成活动至关重要。结果表明，对于人LSP1在细胞中的生发活性，需要在caldesmon-like域和villin headpiece-like域之间进行协作。版权所有2001 Wiley-Liss，Inc.

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