Journal of South China University of Technology (Natural Science Edition) ›› 2016, Vol. 44 ›› Issue (3): 128-135.doi: 10.3969/j.issn.1000-565X.2016.03.018

• Biological Engineering • Previous Articles     Next Articles

Exposition of Phosphotyrosine Site on ITAM-like Motif of ERM Proteins Mediated by Force Through PSGL-1

WU Jian-hua KUANG Xiao-min LIU Wen-ping FANG Ying   

  1. School of Biological Science and Engineering,South China University of Technology,Guangzhou 510006,Guangdong,China
  • Received:2015-09-07 Revised:2015-11-26 Online:2016-03-25 Published:2016-02-02
  • Contact: 方颖(1966-)，女，副教授，主要从事细胞与分子生物力学研究． E-mail:yfang@scut.edu.cn
  • About author:吴建华(1959-) ，男，博士，教授，博士生导师，主要从事细胞与分子生物力学研究．E-mail:wujianhua@scut．edu．cn
  • Supported by:
    Supported by the National Natural Science Foundation of China (31170887，11272125，11432006)

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Abstract: 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.

Key words: PSGL-1, ERM protein, Syk, ITAM-like motif, steered molecular dynamics

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