Protein expression, characterization and activity comparisons of wild type and mutant DUSP5 proteins.

ABSTRACT:

Background

The mitogen-activated protein kinases (MAPKs) pathway is critical for cellular signaling, and proteins such as phosphatases that regulate this pathway are important for normal tissue development. Based on our previous work on dual specificity phosphatase-5 (DUSP5), and its role in embryonic vascular development and disease, we hypothesized that mutations in DUSP5 will affect its function.

Results

In this study, we tested this hypothesis by generating full-length glutathione-S-transferase-tagged DUSP5 and serine 147 proline mutant (S147P) proteins from bacteria. Light scattering analysis, circular dichroism, enzymatic assays and molecular modeling approaches have been performed to extensively characterize the protein form and function. We demonstrate that both prot

SUBMITTER: Nayak J 

PROVIDER: S-EPMC4299175 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature