单位：[1]Experimental Center, Beijing Friendship Hospital, Capital Medical University, Beijing, China医技科室北京市临床医学研究所实验中心首都医科大学附属北京友谊医院[2]National Clinical Research Center for Digestive Disease, Beijing Friendship Hospital, Capital Medical University, Beijing, China首都医科大学附属北京友谊医院[3]Department of Pathology, Beijing Friendship Hospital, Capital Medical University, Beijing, China医技科室病理科病理科首都医科大学附属北京友谊医院[4]Clinical Laboratory Center, Beijing Friendship Hospital, Capital Medical University, Beijing, China医技科室检验科检验科首都医科大学附属北京友谊医院
Cell migration involves dynamic regulation of the actin cytoskeleton, which exhibits rapid actin polymerization at the leading edge of migrating cells. This process relies on regulated recruitment of actin nucleators and actin-binding proteins to the leading edge to polymerize new actin filaments. Many of these proteins have been identified, including the actin-related protein (Arp) 2/3 complex, which has emerged as the core player in the initiation of actin polymerization. However, the functional coordination of these proteins is unclear. Previously, we have demonstrated that the 14-kDa phosphohistidine phosphatase (PHP14) is involved in cell migration regulation and affects actin cytoskeleton reorganization. Here, we show that PHP14 may regulate actin remodeling directly and play an important role in dynamic regulation of the actin cytoskeleton. We observed a colocalization of PHP14 with Arp3 and F-actin at the leading edge of migrating cells. Moreover, PHP14 was recruited to the actin remodeling sites in parallel with Arp3 during lamellipodia formation. Furthermore, PHP14 knockdown impaired Arp3 localization at the leading edge of lamellipodia, as well as lamellipodia formation. Most importantly, we found that PHP14 was a novel F-actin-binding protein, displaying an Arp2/3-dependent localization to the leading edge. Collectively, our results indicated a crucial role for PHP14 in the dynamic regulation of the actin cytoskeleton and cell migration.
基金：
Beijing Talents Fund [2016000021469G227]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81071973]; Wang Bao-En Liver Fibrosis Foundation [20100013]; Rising Star Program from Beijing Friendship Hospital [yyqdkt201516]
第一作者单位：[1]Experimental Center, Beijing Friendship Hospital, Capital Medical University, Beijing, China[2]National Clinical Research Center for Digestive Disease, Beijing Friendship Hospital, Capital Medical University, Beijing, China[*1]Experimental Center, Beijing Friendship Hospital, Capital Medical University, Beijing 100050, China
通讯作者：
通讯机构：[1]Experimental Center, Beijing Friendship Hospital, Capital Medical University, Beijing, China[2]National Clinical Research Center for Digestive Disease, Beijing Friendship Hospital, Capital Medical University, Beijing, China[*1]Experimental Center, Beijing Friendship Hospital, Capital Medical University, Beijing 100050, China
推荐引用方式(GB/T 7714)：
Xu Anjian,Li Xiaojin,Li Siwen,et al.A novel role for 14-kDa phosphohistidine phosphatase in lamellipodia formation[J].CELL ADHESION & MIGRATION.2017,11(5-6):488-495.doi:10.1080/19336918.2016.1268319.
APA：
Xu, Anjian,Li, Xiaojin,Li, Siwen,Sun, Lan,Wu, Shanna...&Huang, Jian.(2017).A novel role for 14-kDa phosphohistidine phosphatase in lamellipodia formation.CELL ADHESION & MIGRATION,11,(5-6)
MLA：
Xu, Anjian,et al."A novel role for 14-kDa phosphohistidine phosphatase in lamellipodia formation".CELL ADHESION & MIGRATION 11..5-6(2017):488-495
