Biopolym. Cell. 2013; 29(5):424-427.
http://dx.doi.org/10.7124/bc.000834
Short Communications
Differential recognition of ITSN2/Ese2 by the SH2 domains of Fyn, Abl1, PLCg1 and PI3KR1 in mouse tissues
1Novokhatska O. V., 1Pankivskyy S. V., 1Dergai M. V., 1Tsyba L. O., 1Rynditch A. V.
  1. State Key Laboratory of Molecular and Cellular Biology
    Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Phosphorylation of endocytic adaptor ITSN2 that enabled its interaction with the SH2 domains of signaling proteins was recently reported. The aim of this study was to determine whether tissue-specific ITSN2 phosphorylation and subsequent recognition by phosphotyrosine-binding domains could occur in mouse tissues. Methods. In silico prediction of interaction motifs, expression of recombinant proteins in bacterial system, GST pull-down analysis, immunoblotting. Results. Analysis of phosphoproteomic data demonstrated tyrosine phosphorylation of mouse ITSN2 homologue, Ese2 protein. Scansite service was used to predict binding motifs for the SH2 domains of Fyn, Abl1, PLCg1 and PI3KR1 within Ese2. Comparison of ITSN2 and Ese2 sequences showed conservation of predicted interaction motifs between human and mouse. GST-fused SH2 domains of Fyn, Abl1, PLCg1 and PI3KR1 were obtained and used as phosphorylation «sensors» of tyrosine-based motifs within Ese2 molecule. Binding of Ese2 to the SH2 domains of Fyn and PLCg1 was observed in brain, lung and heart whereas SH2 domains of Abl1 and PI3KR1 interacted with Ese2 in lung and heart only. Conclusions. Differential Ese2/ SH2 interactions in tissues suggest that tissue-specific tyrosine phosphorylation might regulate specific binding of the Ese2 adaptor to the signaling molecules.
Keywords: ITSN2/Ese2, tyrosine phosphorylation, SH2 domain, tissue-specific interactions
Full text: (PDF, in English)

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