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Blood, 1 June 2005, Vol. 105, No. 11, pp. 4264-4271.
Prepublished online as a Blood First Edition Paper on January 11, 2005; DOI 10.1182/blood-2004-07-2733.
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Submitted July 22, 2004
Accepted January 8, 2005
A systematic scan of interactions with tyrosine motifs in the erythropoietin receptor using a mammalian two-hybrid approach
Tony Montoye, Irma Lemmens, Dominiek Catteeuw, Sven Eyckerman, and Jan Tavernier*
Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology, VIB09, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium
* Corresponding author; email: jan.tavernier{at}UGent.be.
Signalling via the erythropoietin receptor (EpoR) depends on the interaction of several proteins with phosphorylated tyrosine-containing motifs in its cytosolic domain. Detailed mapping of these interactions is required for an accurate insight into Epo signalling. We recently developed MAPPIT (mammalian protein-protein interaction trap), a cytokine-receptor based two-hybrid method that operates in intact Hek293-T mammalian cells. As baits, we used intracellular segments of the EpoR containing one or two tyrosines. Several known signalling molecules including CIS, SOCS2, PI3-K, PLCg and STAT5 were used as prey. We also extended the MAPPIT method to enable interaction analysis with the wild-type EpoR. In this Relay MAPPIT approach, instead of using isolated EpoR fragments as bait, we used the full-length EpoR itself as a receptor-bait. Finally, we introduced MAPPIT in the erythroleukemic TF-1 cell line, which is a more natural setting of the EpoR. With these strategies several known interactions with the EpoR were analysed and evidence for new interactions was obtained.
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