CYTOSKELETON AND SIGNAL TRANSDUCTION IN HOST DEFENSE

描述(改编自研究人员的摘要)：粘附力是一种 吞噬细胞功能的重要调节因子。调查员的长期工作 目的是了解吞噬细胞的激活如何调节整合素- 中介粘连。最近出版的出版物或在媒体上的作品 研究人员实验室证明，L-纤溶酶原(Lpl)是一种F 肌动蛋白捆绑蛋白在SER5上经历增强的磷酸化 对细胞激活的反应。LPL的磷酸化与 整合素介导的增强细胞聚集和/或黏附。 来自LPL氨基末端的多肽模拟了这一效应，并 Ser5的突变消除了这种影响。调查者假设 LPL磷酸化状态对整合素介导的调节作用 粘附力。拟议的研究包括确定 LPL激活整合素功能的机制，测定 整合素激活所需的LPL相互作用，以及 LPL基因敲除小鼠和细胞的特征。

DESCRIPTION (Adapted from the investigator's abstract): Adhesion is an important regulator of phagocyte function. The investigator's long-term goal is to understand how activation of phagocytes regulates integrin- mediated adhesion. Recent publications or work in press from the investigator's laboratory have demonstrated that l-plastin (LPL), an F actin-bundling protein, undergoes enhanced phosphorylation on Ser5 in response to cell activation. LPL phosphorylation is correlated with enhanced cellular aggregation and/or adhesion mediated by integrins. Peptides derived from the amino terminus of LPL mimic this effect and mutation of Ser5 abolishes this effect. The investigator hypothesizes that the state of LPL phosphorylation regulates integrin-mediated adhesion. The proposed studies include the determination of the mechanisms of LPL activation of integrin function, the determination of LPL interactions required for integrin activation, and the characterization of LPL knockout mice and cells.