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J. Biol. Chem., Vol. 280, Issue 7, 5133-5136, February 18, 2005

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R7BP, a Novel Neuronal Protein Interacting with RGS Proteins of the R7 Family^*

Kirill A. Martemyanov, Peter J. Yoo, Nikolai P. Skiba, and Vadim Y. Arshavsky

From the Department of Ophthalmology, Harvard Medical School and the Massachusetts Eye and Ear Infirmary, Boston, Massachusetts 02114

The R7 subfamily of the regulators of G protein signaling (RGS) proteins is represented by four members broadly expressed in the mammalian nervous system. Here we report that in the brain all four R7 proteins form tight complexes with a previously unidentified protein, which we call the R7-binding protein or R7BP. We initially identified R7BP as a protein co-precipitating with the R7 protein, RGS9, from extracts obtained from the striatal region of the brain. We further showed that R7BP forms a tight complex with RGS9 in vitro and that this binding occurs via the N-terminal DEP domain of RGS9. R7BP is expressed throughout the entire central nervous system but not in any of the tested non-neuronal tissues. All four R7 RGS proteins co-precipitate with R7BP from brain extracts and recombinant R7 proteins bind recombinant R7BP with high efficiency. The closest homolog of R7BP is R9AP which was previously found to interact with RGS9 in photoreceptors. Both R7BP and R9AP are related to the syntaxin subfamily of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins involved in vesicular trafficking and exocytosis. In photoreceptors R9AP regulates several critical properties of RGS9 including its intracellular targeting, stability and catalytic activity. This suggests that R7BP interactions with R7 proteins in the brain may also bear major functional significance.

Received for publication, December 20, 2004

^* This work was supported by National Institutes of Health Grant EY-12859 (to V. Y. A.) and by a grant from the Knights Templar Eye Foundation (to K. A. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Ophthalmology, Harvard Medical School, Howe Labs/MEEI, 243 Charles St., Boston, MA 02114. Tel.: 617-573-4371; Fax: 617-573-4290; E-mail: vadim_arshavsky{at}meei.harvard.edu.

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