Ontology highlight
ABSTRACT:
SUBMITTER: Gao K
PROVIDER: S-EPMC4342581 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Gao Kun K Tang Wenwen W Li Yuan Y Zhang Pingzhao P Wang Dejie D Yu Long L Wang Chenji C Wu Dianqing D
Journal of cell science 20150114 5
A hallmark of neutrophil polarization is the back localization of active RHOA and phosphorylated myosin light chain (pMLC, also known as MYL2). However, the mechanism for the polarization is not entirely clear. Here, we show that FAM65B, a newly identified RHOA inhibitor, is important for the polarization. When FAM65B is phosphorylated, it binds to 14-3-3 family proteins and becomes more stable. In neutrophils, chemoattractants stimulate FAM65B phosphorylation largely depending on the signals fr ...[more]