Drep-2 is a novel synaptic protein important for learning and memory

Andlauer, T. F., Scholz-Kornehl, S., Tian, R., Kirchner, M., Babikir, H. A., Depner, H., Loll, B., Quentin, C., Gupta, V. K., Holt, M. G., Dipt, S., Cressy, M., Wahl, M. C., Fiala, A., Selbach, M., Schwarzel, M., Sigrist, S. J. (November 2014) Drep-2 is a novel synaptic protein important for learning and memory. Elife, 3. ISSN 2050-084x

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URL: http://www.ncbi.nlm.nih.gov/pubmed/25392983

DOI: 10.7554/eLife.03895

Abstract

CIDE-N domains mediate interactions between the DNase Dff40/CAD and its inhibitor Dff45/ICAD. In this study, we report that the CIDE-N protein Drep-2 is a novel synaptic protein important for learning and behavioral adaptation. Drep-2 was found at synapses throughout the Drosophila brain and was strongly enriched at mushroom body input synapses. It was required within Kenyon cells for normal olfactory short- and intermediate-term memory. Drep-2 colocalized with metabotropic glutamate receptors (mGluRs). Chronic pharmacological stimulation of mGluRs compensated for drep-2 learning deficits, and drep-2 and mGluR learning phenotypes behaved non-additively, suggesting that Drep 2 might be involved in effective mGluR signaling. In fact, Drosophila fragile X protein mutants, shown to benefit from attenuation of mGluR signaling, profited from the elimination of drep-2. Thus, Drep-2 is a novel regulatory synaptic factor, probably intersecting with metabotropic signaling and translational regulation.

Item Type:	Paper
Subjects:	organism description > animal > insect > Drosophila organism description > animal behavior > learning organism description > animal behavior > memory organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > synaptic transmission
CSHL Authors:	Cressy, Michael
Communities:	CSHL labs > Dubnau lab
Depositing User:	Matt Covey
Date:	13 November 2014
Date Deposited:	21 Nov 2014 16:41
Last Modified:	16 Jul 2021 16:02
PMCID:	PMC4229683
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/30923

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