scholarly journals Dual-Specificity Phosphatase 10 Controls Brown Adipocyte Differentiation by Modulating the Phosphorylation of P38 Mitogen-Activated Protein Kinase

PLoS ONE ◽  
2013 ◽  
Vol 8 (8) ◽  
pp. e72340 ◽  
Author(s):  
Hye-Ryung Choi ◽  
Won Kon Kim ◽  
Eun Young Kim ◽  
Baek Soo Han ◽  
Jeong-Ki Min ◽  
...  
2020 ◽  
Author(s):  
Ganesan Senthil Kumar ◽  
Rebecca Page ◽  
Wolfgang Peti

AbstractThe sequence-specific backbone assignment of the mitogen-activated protein kinase (MAPK) binding domain of the dual-specificity phosphatase 1 (DUSP1) has been accomplished using a uniformly [13C,15N]-labeled protein. These assignments will facilitate further studies of DUSP1 in the presence of inhibitors/ligands to target MAPK associated diseases and provide further insights into the function of dual-specificity phosphatase 1 in MAPK regulation.


Author(s):  
George T. Lountos ◽  
Brian P. Austin ◽  
Joseph E. Tropea ◽  
David S. Waugh

Human dual-specificity phosphatase 7 (DUSP7/Pyst2) is a 320-residue protein that belongs to the mitogen-activated protein kinase phosphatase (MKP) subfamily of dual-specificity phosphatases. Although its precise biological function is still not fully understood, previous reports have demonstrated that DUSP7 is overexpressed in myeloid leukemia and other malignancies. Therefore, there is interest in developing DUSP7 inhibitors as potential therapeutic agents, especially for cancer. Here, the purification, crystallization and structure determination of the catalytic domain of DUSP7 (Ser141–Ser289/C232S) at 1.67 Å resolution are reported. The structure described here provides a starting point for structure-assisted inhibitor-design efforts and adds to the growing knowledge base of three-dimensional structures of the dual-specificity phosphatase family.


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