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Mol. Cell. Biol. doi:10.1128/MCB.02014-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Deciphering the crosstalk between hnRNP K and c-Src: The c-Src activation domain in hnRNP K is distinct from a second interaction site

Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany

^* To whom correspondence should be addressed. Email: dostareck{at}biochemtech.uni-halle.de. aostareck{at}biochemtech.uni-halle.de.

	Abstract

The protein tyrosine kinase c-Src is regulated by two intramolecular interactions. The repressed state is achieved through interaction of the SH2 domain with the phosphorylated C-terminal tail and association of the SH3 domain with a poly-proline type II helix formed by the linker region between SH2 and kinase domain. HnRNP K, the founding member of the KH-domain protein family, is involved in chromatin remodeling, regulation of transcription and translation of specific mRNAs and is a target in different signal transduction pathways. In particular it functions as a specific activator and a substrate of the tyrosine kinase c-Src. Here we address the question how hnRNP K interacts with and activates c-Src. We define the proline residues in hnRNP K in the proline-rich motifs P2(aa285-297) and P3(aa303-318) that are necessary and sufficient for the specific activation of c-Src and dissect the amino acid sequence (aa216-226) of hnRNP K that mediates a second interaction with c-Src. Our findings indicate that the interaction with c-Src and the activation of the kinase are separable functions of hnRNP K. HnRNP K acts as a scaffold protein that integrates signaling cascades by facilitating the cross-talk between kinases and factors that mediate nucleic acid directed processes.

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