Interactions with the Abelson tyrosine kinase reveal compartmentalization of eyes absent function between nucleus and cytoplasm. Dev Cell 2009 Feb;16(2):271-9
Date
02/17/2009Pubmed ID
19217428Pubmed Central ID
PMC2670569DOI
10.1016/j.devcel.2008.12.005Scopus ID
2-s2.0-59649130295 (requires institutional sign-in at Scopus site) 50 CitationsAbstract
Eyes absent (Eya), named for its role in Drosophila eye development but broadly conserved in metazoa, possesses dual functions as a transcriptional coactivator and protein tyrosine phosphatase. Although Eya's transcriptional activity has been extensively characterized, the physiological requirements for its phosphatase activity remain obscure. In this study, we provide insight into Eya's participation in phosphotyrosine-mediated signaling networks by demonstrating cooperative interactions between Eya and the Abelson (Abl) tyrosine kinase during development of the Drosophila larval visual system. Mechanistically, Abl-mediated phosphorylation recruits Eya to the cytoplasm, where in vivo studies reveal a requirement for its phosphatase function. Thus, we propose a model in which, in addition to its role as a transcription factor, Eya functions as a cytoplasmic protein tyrosine phosphatase.
Author List
Xiong W, Dabbouseh NM, Rebay IMESH terms used to index this publication - Major topics in bold
AnimalsAxons
Cell Nucleus
Cytoplasm
Developmental Biology
Drosophila Proteins
Drosophila melanogaster
Eye Proteins
Gene Expression Regulation, Enzymologic
Genotype
Models, Biological
Models, Genetic
Phosphorylation
Protein-Tyrosine Kinases
Signal Transduction
Transcription, Genetic
