Structure, Function and Modulation of Striatal-enriched Protein Tyrosine Phosphatase (STEP)

Title:Structure, Function and Modulation of Striatal-enriched Protein Tyrosine Phosphatase (STEP)

Volume: 28 Issue: 37

Author(s): Xiao Liang, Xuben Hou* Hao Fang*

Affiliation:

• Key Laboratory of Chemical Biology (Ministry of Education), School of Pharmaceutical Science, Cheeloo College of Medicine, Shandong University, Ji’nan, Shandong 250012,China

• Key Laboratory of Chemical Biology (Ministry of Education), School of Pharmaceutical Science, Cheeloo College of Medicine, Shandong University, Ji’nan, Shandong 250012,China

Keywords: Striatal-enriched protein tyrosine phosphatase, nervous system diseases, inhibitor, activator, structureactivity relationships, PTP domain.

Abstract: Striatal-enriched protein tyrosine phosphatase (STEP) is exclusively expressed in the central nervous system and regulates various neuronal signaling factors through the dephosphorylation of different substrates. Dysregulated expression or uncontrollable enzymatic activity of STEP contributes to neurological disorders such as Alzheimer's disease, which makes it a promising pharmaceutical target. Herein, we have reviewed the structure and biological functions of STEP, as well as the recent development of smallmolecule STEP modulators. We hope this review will provide a reference for the further development of more potent and selective STEP inhibitors for the treatment of nervous system diseases.

Cite this article as:

Liang Xiao , Hou Xuben *, Fang Hao *, Structure, Function and Modulation of Striatal-enriched Protein Tyrosine Phosphatase (STEP), Current Medicinal Chemistry 2021; 28 (37) . https://dx.doi.org/10.2174/0929867328666210412123304