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J. Biol. Chem., Vol. 283, Issue 41, 27494-27503, October 10, 2008

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Interplay of the Ca²⁺-binding Protein DREAM with Presenilin in Neuronal Ca²⁺ Signaling^*

Laura Fedrizzi, Dmitry Lim^¶, Ernesto Carafoli^¶, and Marisa Brini¹

From the Departments of Biochemistry and Experimental Veterinary Sciences, University of Padova, Padova 35131, Italy and the ^¶Venetian Institute of Molecular Medicine, Padova 35129, Italy

The Ca²⁺-binding protein DREAM regulates gene transcription and Kv potassium channels in neurons but has also been claimed to interact with presenilins, which are involved in the generation of β-amyloid and in the regulation of the Ca²⁺ content in the endoplasmic reticulum. The role of DREAM in Ca²⁺ homeostasis was thus explored in SH-SY5Y cells stably or transiently overexpressing DREAM or a Ca²⁺-insensitive mutant of it. The overexpression of DREAM had transcriptional and post-transcriptional effects. Endoplasmic reticulum Ca²⁺ and capacitative Ca²⁺ influx were reduced in stably expressing cells. The previously shown down-regulation of Na⁺/Ca²⁺ exchanger 3 expression was confirmed; it could cause a local increase of subplasma membrane Ca²⁺ and thus inhibit capacitative Ca²⁺ influx. DREAM up-regulated the expression of the inositol 1,4,5-trisphosphate receptor and could thus increase the unstimulated release of Ca²⁺ through it. The transient coexpression of DREAM and presenilin potentiated the decrease of endoplasmic reticulum Ca²⁺ observed in presenilin-overexpressing cells. This could be due to a direct effect of DREAM on presenilin as the two proteins interacted in a Ca²⁺-independent fashion.

Received for publication, May 30, 2008 , and in revised form, July 21, 2008.

^* The work was supported by Telethon Foundation Project GGP04169 (to M. B.), Italian Ministry of University and Research Grant PRIN 2003 and 2005 (to M. B.), and FP6 program of the European Union FP6 Integrated Projects NeuroNe and LSH-2003-2.1.3-3 (to E. C.). 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 To whom correspondence should be addressed: Dept. of Biochemistry, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy. Tel.: 39-049-8276167; Fax: 39-049-8276125; E-mail: marisa.brini{at}unipd.it.

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