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J. Biol. Chem., Vol. 275, Issue 41, 32129-32134, October 13, 2000

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The  Subunits of G_z and G_i Interact with the eyes absent Transcription Cofactor Eya2, Preventing Its Interaction with the Six Class of Homeodomain-containing Proteins^*

Xiaomin Fan, Lawrence F. Brass^§, Mortimer Poncz^¶, François Spitz, Pascal Maire, and David R. Manning^**

From the Departments of  Pharmacology, ^§ Medicine and Pathology, and ^¶ Pediatrics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and the  Institut Cochin de Génétique Moléculaire, INSERM U129, Université René Descartes, 75014 Paris, France

Yeast two-hybrid techniques were used to identify possible effectors for the heterotrimeric G protein G_z in human bone marrow cells. Eya2, a human homologue of the Drosophila Eya transcription co-activator, was identified. Eya2 interacts with activated G_z and at least one other member of the G_i family, G_i2. Interactions were confirmed in mammalian two-hybrid and glutathione S-transferase fusion protein pull-down assays. Regions of Eya2-mediating interaction were mapped to the C-terminal Eya consensus domain. Eya2 is an intrinsically cytosolic protein that is translocated to the nucleus by members of the Six homeodomain-containing family of proteins. Activated G_z and G_i2 prevent Eya2 translocation and inhibit Six/Eya2-mediated activation of a reporter gene controlled through the MEF3/TATA promoter. Although G proteins are known to regulate the activity of numerous transcription factors, this regulation is normally achieved indirectly via one or more intermediates. We show here a novel functional regulation of a co-activator directly by G protein subunits.

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