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The novel SAM domain protein Aveugle is required for Raf activation in the Drosophila EGF receptor signaling pathway

Skirball Institute for Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA

Activation of the Raf kinase by GTP-bound Ras is a poorly understood step in receptor tyrosine kinase signaling pathways. One such pathway, the epidermal growth factor receptor (EGFR) pathway, is critical for cell differentiation, survival, and cell cycle regulation in many systems, including the Drosophila eye. We have identified a mutation in a novel gene, aveugle, based on its requirement for normal photoreceptor differentiation. The phenotypes of aveugle mutant cells in the eye and wing imaginal discs resemble those caused by reduction of EGFR pathway function. We show that aveugle is required between ras and raf for EGFR signaling in the eye and for mitogen-activated protein kinase phosphorylation in cell culture. aveugle encodes a small protein with a sterile motif (SAM) domain that can physically interact with the scaffold protein connector enhancer of Ksr (Cnk). We propose that Aveugle acts together with Cnk to promote Raf activation, perhaps by recruiting an activating kinase.

[Keywords: Raf; MAP kinase; receptor tyrosine kinase; EGFR; photoreceptor; SAM]

Received November 4, 2005; revised version accepted January 24, 2006.

² Institut de Biologie du Développement de Marseille, Campus de Luminy, Case 907, 13288 Marseille Cedex 9, France.

³ Corresponding author.

E-MAIL treisman{at}saturn.med.nyu.edu; FAX (212) 263-7760.

Supplemental material is available at http://www.genesdev.org.

Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1390506

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