Structural characterization of the PIT-1/ ETS-1 interaction: PIT-1 phosphorylation regulates PIT-1/ ETS-1 binding

K.D. Augustijn, D.L. Duval, R.W. Wechselberger, R. Kaptein, A. Gutierrez-Hartmann, P.C. van der Vliet

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The POU-domain transcription factor Pit-1 and Ets-1, a member of the ETS family of transcription factors, can associate in solution and synergistically activate the prolactin promoter by binding to a composite response element in the prolactin promoter. We mapped the minimal region of Ets-1 required for the interaction with the Pit-1 POU-homeodomain. Here, we describe a detailed NMR study of the interaction between the POU-homeodomain of Pit-1 and the minimal interacting region of Ets-1. By using heteronuclear single quantum coherence titration experiments, we were able to map exact residues on the POU-homeodomain that are involved in the interaction with this minimal Ets-1 interaction domain. By using ourNMRdata, we generated point mutants in the POU-homeodomain and tested their effect on the interaction with Ets-1. Our results show that phosphorylation of Pit-1 can regulate the interaction with Ets-1.
Original languageUndefined/Unknown
Pages (from-to)12657-12662
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number20
Publication statusPublished - 2002

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