炎症反应阶段，P-选择素糖蛋白配体 1(PSGL-1)与埃兹蛋白/根蛋白/膜突蛋白(EＲM)的结合在招募脾酪氨酸激酶(Syk)并促进白细胞激活中发挥了重要作用． 文中通过晶体结构分析发现，位于 ERM 蛋白非传统的免疫受体酪氨酸活化基序(ITAM-like)上的两个磷酸化位点(Y191 和 Y205)周围存在较大的空间位阻，这将阻碍其被 Src 家族激酶酪氨酸磷酸化继而招募 Syk 的过程． 文中用拉伸分子动力学模拟的方法模拟力学环境下 PSGL-1 与根蛋白 FERM 结构域的相互作用，构象分析和残基溶剂可及表面积的变化都表明，经由 PSGL-1 传导的力学信号可以介导根蛋白 ITAM-like 序列上磷酸化位点 Y205的暴露． 文中结果揭示了一条经由 PSGL-1 胞内域激活 Syk 的力学信号通路，并且在原子层面上对 PSGL-1/ERM/Syk 之间的相互作用给予了阐释．

P-selectin glycoprotein ligand 1 (PSGL-1) engaged by ezrin-radixin-moesin (ERM) proteins plays an important role in recruiting spleen tyrosine kinase (Syk) and activating leukocyte in the process of inflammatory re- sponse.Firstly,the crystal structure of radixin FERM domain indicates that the steric effect on ITAM-like motif and phosphorylation sites (Y191 and Y205) can hamper their phosphorylation by Src family tyrosine kinase and their combination with Syk.Then,steered molecular dynamics (SMD) simulation is carried out to explore the interaction between the complex of PSGL-1 juxtamembrane peptide and radixin FERM domain under force load.Both conforma- tion analysis and solvent accessible surface variant show that the mechanical signal transmitting through PSGL-1 cy- toplasmic region can mediate the exposition of phosphotyrosine site Y205 on ITAM-like motif of radixin.The results of this study present a mechanical signal pathway from PSGL-1 cytoplasmic region to Syk and expound the interac- tion mechanism of PSGL-1/ERM/Syk at atomic level.