Author Correction: Eya3 partners with PP2A to induce c-Myc stabilization and tumor progression.

In the original version of this Article, the title of the legend to Fig. 7 incorrectly read 'Knockdown of B55α increases breast cancer metastasis' instead of 'Knockdown of B55α decreases breast cancer metastasis'. This has now been corrected in both the PDF and HTML versions of the Article.

Eya3 partners with PP2A to induce c-Myc stabilization and tumor progression.

Eya genes encode a unique family of multifunctional proteins that serve as transcriptional co-activators and as haloacid dehalogenase-family Tyr phosphatases. Intriguingly, the N-terminal domain of Eyas, which does not share sequence similarity to any known phosphatases, contains a separable Ser/Thr phosphatase activity. Here, we demonstrate that the Ser/Thr phosphatase activity of Eya is not intrinsic, but arises from its direct interaction with the protein phosphatase 2A (PP2A)-B55α holoenzyme.

The Eya phosphatase: Its unique role in cancer.

The Eya proteins were originally identified as essential transcriptional co-activators of the Six family of homeoproteins. Subsequently, the highly conserved C-terminal domains of the Eya proteins were discovered to act as a Mg-dependent Tyr phosphatases, making Eyas the first transcriptional activators to harbor intrinsic phosphatase activity. Only two direct targets of the Eya Tyr phosphatase have been identified: H2AX, whose dephosphorylation directs cells to the DNA repair instead of the apoptotic pathway upon DNA damage, and ERβ, whose dephosphorylation inhibits its anti-tumor transcriptional activity.