Studying the regulation of MAP Kinase by MAP Kinase phosphatases in vitro and in cell systems.
Signaling through MAPK pathways involves a network of activating kinases and inactivating phosphatases. While single MAPK kinases account for specific activation of the distinct MAPKs, inactivation of MAPKs by phosphatases involves a wider spectrum of enzymes, with phosphatases from distinct families displaying specificity toward MAPKs. The dual-specificity family of MAPK phosphatases, MKPs, constitutes the major group of MAPK inactivating phosphatases. MKPs are widely expressed, in a tissue- and development-regulated manner, and the control of their expression and function is crucial for the regulation of MAPK signaling. Here, we present three methods to analyze the regulation of MAPKs by MKPs, using transient and stable-inducible MKP overexpression cell systems and in vitro phosphatase experiments.
Tárrega
Céline
C
Centro de Investigación Príncipe Felipe, Valencia, Spain.
Nunes-Xavier
Caroline
C
Cejudo-Marín
Rocío
R
Martín-Pérez
Jorge
J
Pulido
Rafael
R
D000818:Animals; D045744:Cell Line, Tumor; D057075:Enzyme Assays / Q000379:methods*; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D006801:Humans; D054639:Mitogen-Activated Protein Kinase Phosphatases / Q000378:metabolism*; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D013752:Tetracycline / Q000494:pharmacology
D020928:Mitogen-Activated Protein Kinases; D054639:Mitogen-Activated Protein Kinase Phosphatases; D013752:Tetracycline