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J. Biol. Chem., Vol. 283, Issue 3, 1597-1600, January 18, 2008

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The Stargazin C Terminus Encodes an Intrinsic and Transferable Membrane Sorting Signal^*

From the Department of Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80523-1617

Activity-dependent plasticity of -amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptors is regulated by their auxiliary subunit, stargazin. Association with stargazin enhances -amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor surface expression and modifies the receptor's biophysical properties. Fusing the cytoplasmic C terminus of stargazin to the C-terminal domains of either GluR1 or the gonadotropin-releasing hormone receptor permits efficient trafficking from the endoplasmic reticulum and sorting to the basolateral membrane without altering other properties of either receptor.

Received for publication, October 1, 2007

^* 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.

¹ Present address: Dept. of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02912.

² To whom correspondence should be addressed. Tel.: 970-491-1563; Fax: 970-491-7907; E-mail: kathy.partin{at}research.colostate.edu.

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