Allosteric inhibitors of the Eya2 phosphatase are selective and inhibit Eya2-mediated cell migration.

ABSTRACT: Eya proteins are essential co-activators of the Six family of transcription factors and contain a unique tyrosine phosphatase domain belonging to the haloacid dehalogenase family of phosphatases. The phosphatase activity of Eya is important for the transcription of a subset of Six1-target genes, and also directs cells to the repair rather than apoptosis pathway upon DNA damage. Furthermore, Eya phosphatase activity has been shown to mediate transformation, invasion, migration, and metastasis of breast cancer cells, making it a potential new drug target for breast cancer. We have previously identified a class of N-arylidenebenzohydrazide compounds that specifically inhibit the Eya2 phosphatase. Herein, we demonstrate that these compounds are reversible inhibitors that selectively inhibit th

SUBMITTER: Krueger AB 

PROVIDER: S-EPMC4047403 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature