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Updated: May 30, 2026

Mouse Eye Enucleation for Remote High-throughput Phenotyping
Published on: November 19, 2011
Characterization of the threonine-phosphatase of mouse eyes absent 3
Teruyuki Sano1, Shigekazu Nagata
1Department of Medical Chemistry, Graduate School of Medicine, Kyoto University, Yoshida-Konoe, Kyoto, Japan.
Abstract:
Eyes absent (EYA) has tyrosine- and threonine-phosphatase activities in their C-terminal and N-terminal regions, respectively. Using various mutants of mouse EYA3, we showed that the 68-amino acid domain between positions 53 and 120 was necessary and sufficient for its threonine-phosphatase activity. Point mutations were then introduced, and residues Cys-56, Tyr-77, His-79, and Tyr-90 were essential for the EYA3s threonine-phosphatase. The 68-amino acid domain is not well conserved among the four mouse EYA members, but is evolutionally highly conserved in the orthologous EYA members of different species, suggesting that the threonine-phosphatase of EYA3 has a function distinct from that of the other EYAs.

