The transcription factor Eyes absent is a protein tyrosine phosphatase

Tina L. Tootle, Serena J. Silver, Erin L. Davies, Victoria Newman, Robert R. Latek, Ishara A. Mills, Jeremy D. Selengut, Beth E. W. Parlikar and Ilaria Rebay ()
Additional contact information
Tina L. Tootle: Whitehead Institute for Biomedical Research
Serena J. Silver: Whitehead Institute for Biomedical Research
Erin L. Davies: Whitehead Institute for Biomedical Research
Victoria Newman: Whitehead Institute for Biomedical Research
Robert R. Latek: Whitehead Institute for Biomedical Research
Ishara A. Mills: Whitehead Institute for Biomedical Research
Jeremy D. Selengut: The Institute for Genomic Research
Beth E. W. Parlikar: Whitehead Institute for Biomedical Research
Ilaria Rebay: Whitehead Institute for Biomedical Research

Nature, 2003, vol. 426, issue 6964, 299-302

Abstract: Abstract Post-translational modifications provide sensitive and flexible mechanisms to dynamically modulate protein function in response to specific signalling inputs1. In the case of transcription factors, changes in phosphorylation state can influence protein stability, conformation, subcellular localization, cofactor interactions, transactivation potential and transcriptional output1. Here we show that the evolutionarily conserved transcription factor Eyes absent (Eya)2,3 belongs to the phosphatase subgroup of the haloacid dehalogenase (HAD) superfamily4,5, 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.

Date: 2003
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature02097 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:426:y:2003:i:6964:d:10.1038_nature02097

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature02097

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().