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Citation
Tootle, T.L., Silver, S.J., Davies, E.L., Newman, V., Latek, R.R., Mills, I.A., Selengut, J.D., Parlikar, B.E., Rebay, I. (2003). The transcription factor Eyes absent is a protein tyrosine phosphatase.  Nature 426(6964): 299--302.
FlyBase ID
FBrf0167928
Publication Type
Research paper
Abstract

Post-translational modifications provide sensitive and flexible mechanisms to dynamically modulate protein function in response to specific signalling inputs. In the case of transcription factors, changes in phosphorylation state can influence protein stability, conformation, subcellular localization, cofactor interactions, transactivation potential and transcriptional output. Here we show that the evolutionarily conserved transcription factor Eyes absent (Eya) belongs to the phosphatase subgroup of the haloacid dehalogenase (HAD) superfamily, and propose a function for it as a non-thiol-based protein tyrosine phosphatase. Experiments performed in cultured Drosophila cells and in vitro indicate that Eyes absent has intrinsic protein tyrosine phosphatase activity and can autocatalytically dephosphorylate itself. Confirming the biological significance of this function, mutations that disrupt the phosphatase active site severely compromise the ability of Eyes absent to promote eye specification and development in Drosophila. Given the functional importance of phosphorylation-dependent modulation of transcription factor activity, this evidence for a nuclear transcriptional coactivator with intrinsic phosphatase activity suggests an unanticipated method of fine-tuning transcriptional regulation.

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PubMed Central ID
Related Publication(s)
Note

Signal transduction: an eye on organ development.
Epstein and Neel, 2003, Nature 426(6964): 238--239 [FBrf0173111]

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Secondary IDs
  • FBrf0173113
Language of Publication
English
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Parent Publication
Publication Type
Journal
Abbreviation
Nature
Title
Nature
Publication Year
1869-
ISBN/ISSN
0028-0836
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