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The Journal of Neuroscience, October 15, 2002, 22(20):8827-8837

A Receptor for Activated C Kinase Is Part of Messenger Ribonucleoprotein Complexes Associated with PolyA-mRNAs in Neurons

Frank Angenstein¹, Anne M. Evans², Robert E. Settlage^{2, 4}, Stewart T. Moran¹, Shuo-Chien Ling¹, Anna Y. Klintsova¹, Jeffrey Shabanowitz², Donald F. Hunt^{2, 3}, and William T. Greenough¹

¹ Beckman Institute/Neuronal Pattern Analysis, University of Illinois, Urbana, Illinois 61801, Departments of ² Chemistry and ³ Pathology, University of Virginia, Charlottesville, Virginia 22904, and ⁴ ProteoMS, LLC, Charlottesville, Virginia 22903

Long-lasting changes in synaptic functions after an appropriate stimulus require altered protein expression at the synapse. To restrict changes in protein composition to activated synapses, proteins may be synthesized locally as a result of transmitter receptor-triggered signaling pathways. Second messenger-controlled mechanisms that affect mRNA translation are essentially unknown. Here we report that a receptor for activated C kinase, RACK1, is a component of messenger ribonucleoprotein (mRNP) complexes. RACK1 is predominantly associated with polysome-bound, polyA-mRNAs that are being actively translated. We find it to be present in a complex with -tubulin and at least two mRNA-binding proteins, polyA-binding protein 1 and a 130 kDa polyA-mRNA binding protein (KIAA0217). Activation of PKC2 in vitro by phosphatidylserine/diacylglycerol or in hippocampal slices by metabotropic glutamate receptor stimulation increased the amount of RACK1/PKC2 associated with polysome-bound polyA-mRNAs. In vitro, PKC2 can phosphorylate a subset of polyA-mRNA-associated proteins that are also phosphorylated under in vivo conditions. On the basis of these findings plus the somatodendritic localization of RACK1, we hypothesize that metabotropic glutamate receptor-triggered binding of activated PKC2 to mRNP complexes bound to polyA-mRNAs is involved in activity-triggered control of protein synthesis.

Key words: translational control; messenger ribonucleoproteins; metabotropic glutamate receptor; protein kinase C; protein phosphorylation; polyA-mRNA; mass spectrometry

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Copyright © 2002 Society for Neuroscience  0270-6474/02/22208827-11$05.00/0

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