Metabotropic glutamate receptor-initiated translocation of protein kinase p90rsk to polyribosomes: a possible factor regulating synaptic protein synthesis.
Maintenance of lasting synaptic efficacy changes requires protein synthesis. We report here a mechanism that might influence translation control at the level of the single synapse. Stimulation of metabotropic glutamate receptors in hippocampal slices induces a rapid protein kinase C-dependent translocation of multifunction kinase p90rsk to polyribosomes; concomitantly, there is enhanced phosphorylation of at least six polyribosome binding proteins. Among the polyribosome bound proteins are the p90rsk-activating kinase ERK-2 and a known p90rsk substrate, glycogen synthase kinase 3beta, which regulates translation efficiency via eukaryotic initiation factor 2B. Thus metabotropic glutamate receptor stimulation could induce synaptic activity-dependent translation via translocation of p90rsk to ribosomes.
Angenstein
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Department of Beckman Institute, University of Illinois, Urbana-Champaign, IL 61801, USA. angenste@uiuc.edu
Greenough
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WT
Weiler
I J
IJ
D000818:Animals; D001692:Biological Transport; D006624:Hippocampus / Q000502:physiology*; D009419:Nerve Tissue Proteins / Q000096:biosynthesis; D010766:Phosphorylation; D011132:Polyribosomes / Q000502:physiology*; D051381:Rats; D020318:Rats, Long-Evans; D017470:Receptors, Glutamate / Q000502:physiology*; D019893:Ribosomal Protein S6 Kinases / Q000378:metabolism*; D013569:Synapses / Q000502:physiology*
D009419:Nerve Tissue Proteins; D017470:Receptors, Glutamate; D019893:Ribosomal Protein S6 Kinases