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J. Biol. Chem., Vol. 282, Issue 52, 37783-37793, December 28, 2007

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Components of the Translational Machinery Are Associated with Juvenile Glycine Receptors and Are Redistributed to the Cytoskeleton upon Aging and Synaptic Activity^*

Raphael Bluem¹, Enrico Schmidt¹², Carsten Corvey, Michael Karas, Andrea Schlicksupp, Joachim Kirsch, and Jochen Kuhse³

From the Department of Anatomy and Cell Biology, University of Heidelberg, Im Neuenheimer Feld 307, 69120 Heidelberg and the Department of Pharmaceutical Chemistry, University of Frankfurt, Max-von-Laue-Strasse 9, D-60438 Frankfurt, Germany

The translation eukaryotic elongation factor 1 (eEF1A) is a monomeric GTPase involved in protein synthesis. In addition, this protein is thought to participate in other cellular functions such as actin bundling, cell cycle regulation, and apoptosis. Here we show that eEF1A is associated with the 2 subunit of the inhibitory glycine receptor in pulldown experiments with rat brain extracts. Moreover, additional proteins involved in translation like ribosomal S6 protein and p70 ribosomal S6 protein kinase as well as ERK1/2 and calcineurin were identified in the same pulldown approaches. Glycine receptor activation in spinal cord neurons cultured for 1 week resulted in an increased phosphorylation of ribosomal S6 protein. Immunocytochemistry showed that eEF1A and ribosomal S6 protein are localized in the soma, dendrites, and at synapses of cultured hippocampal and spinal cord neurons. Consistent with our biochemical data, immunoreactivities of both proteins were partially overlapping with glycine receptor immunoreactivity in cultured spinal cord and hippocampal neurons. After 5 weeks in culture, eEF1A immunoreactivity was redistributed to the cytoskeleton in about 45% of neurons. Interestingly, the degree of redistribution could be increased at earlier stages of in vitro differentiation by inhibition of either the ERK1/2 pathway or glycine receptors and simultaneous N-methyl-D-aspartate receptor activation. Our findings suggest a functional coupling of eEF1A with both inhibitory and excitatory receptors, possibly involving the ERK-signaling pathway.

Received for publication, October 5, 2007

^* This work was supported by Deutsche Forschungsgemeinschaft Grant Ku 856/5-3 and Forschergruppe 577. 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 Both authors contributed equally to this work.

² Present address: BioIII, Bioinformatics and Molecular Genetics, Schaenzlestrasse 1, D-79104 Freiburg, Germany.

³ To whom correspondence should be addressed. Tel.: 49-6221-548663; Fax: 49-6221-544952; E-mail: jochen.kuhse{at}urz.uni-heidelberg.de.

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