Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase (pages 315–329)
Rong Li, Di-Dong Xie, Jun-hong Dong, Hui Li, Kang-shuai Li, Jing Su, Lai-Zhong Chen, Yun-Fei Xu, Hong-Mei Wang, Zheng Gong, Guo-Ying Cui, Xiao Yu, Kai Wang, Wei Yao, Tao Xin, Min-Yong Li, Kun-Hong Xiao, Xiao-fei An, Yuqing Huo, Zhi-gang Xu, Jin-Peng Sun and Qi Pang
Version of Record online: 31 OCT 2013 | DOI: 10.1111/jnc.12463
Regulation of phospho-ERK by STEP underlies important neuronal activities. A detailed enzymologic characterisation and cellular studies of STEP revealed that specific residues in KIM and active site mediated ERK recognition. Structural differences between the KIM-ERK interfaces and the active site among different ERK phosphatases could be targeted to develop specific STEP inhibitor, which has therapeutic potential for neurological disorders. PKA, protein kinase A & NGF, nerve growth factor.
Vol. 134, Issue 5, 978, Version of Record online: 14 JUL 2015