Structural mechanism underlying regulation of human EFhd2/Swiprosin-1 actin-bundling activity by Ser183 phosphorylation

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• 作者：Kyoung Ryoung Park^a ; ^b ; Jun Yop An^a ; ^b ; Jung Youn Kang^a ; ^b ; Jung-Gyu Lee^a ; ^b ; Youngjin Lee^a ; ^b ; Sang A Mun^a ; ^b ; Chang-Duk Jun^a ; Woo Keun Song^a ; Soo Hyun Eom^a ; ^b ; ^c ; ^{eom@gist.ac.kr}
• 关键词：EFhd2/Swiprosin-1 ; F-actin-bundling protein ; Crystal structure ; Phosphorylation
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：29 January 2017
• 年：2017
• 卷：483
• 期：1
• 页码：442-448
• 全文大小：1867 K
• 卷排序：483

文摘

EFhd2 is an actin-binding protein in the central nervous and immune systems of mammals. We created a core domain phospho-mimicking mutant of the EFhd2 (CDEFhd2S183E). The crystal structure of CDEFhd2S183E was solved at 1.86 Å. S183E changes the conformational dynamics and the surface charge distribution of the actin-binding sites. We propose a model for the phosphorylation-dependent modulation of actin dynamics by EFhd2.