The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes (original) (raw)

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Published: 23 April 1998

Oncogene volume 16, pages 1779–1788 (1998)Cite this article

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Abstract

c-Abl, the non-receptor tyrosine kinase is associated with EP, a DNA element found in promoters/enhancers of different viruses and cell-cycle regulated genes. EP-DNA binds RFXI, a member of a novel family of DNA-binding proteins that is conserved through evolution and in yeast, it controls differentiation and exit from the mitotic cycle to G0. EP-associated proteins are preferentially tyrosine phosphorylated and the associated c-Abl has strong tyrosine kinase activity. Here we investigated the molecular mechanism underlying this c-Abl kinase activity. We show that RFXI and c-Abl are in direct interaction, in vitro and in cell extracts, through the RFXI proline rich (PxxP) motif and the c-Abl SH3 domain. Remarkably, this interaction significantly potentiates c-Abl but not v-Abl auto-kinase activity. Collectively, we describe a novel mechanism of c-Abl recruitment to a defined DNA-cis element with its concomitant kinase activation. We propose that this mechanism may act to regulate cell-cycle control genes.

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Authors and Affiliations

Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Reuven Agami & Yosef Shaul

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Reuven Agami
Yosef Shaul

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Agami, R., Shaul, Y. The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes.Oncogene 16, 1779–1788 (1998). https://doi.org/10.1038/sj.onc.1201708

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Received: 18 September 1997
Revised: 07 November 1997
Accepted: 07 November 1997
Published: 23 April 1998
Issue Date: 09 April 1998
DOI: https://doi.org/10.1038/sj.onc.1201708