Dendritic and postsynaptic protein synthetic machinery

Abstract

There is a growing body of evidence that local protein synthesis beneath synapses may provide a novel mechanism underlying plastic phenomena. In vivo and in vitro biochemical data show that dendrites can perform translation and glycosylation. Using antibodies directed against the eukaryotic protein synthetic machinery, we sought to identify the structures implicated in nonperinuclear translation, namely dendritic and postsynaptic protein synthesis. We performed a morphological and immunocytochemical analysis of ventromedial horn rat spinal cord neurons using both light and electron microscopy. We show at the cellular level that, in vivo, protein synthesis macrocomplexes (ribosomes and elF-2) as well as the endomembranous system implicated in cotranslational and posttranslational modifications (endoplasmic reticulum and Golgi cisternae) penetrated some dendrites. Membrane-limited organelles of different shape and size are present close to the postsynaptic differentiations of most synapses, independently of their localization on the neuronal surface. We demonstrate (1) that some cisternae are immunoreactive for antibodies against ribosomal proteins and elF-2, and (2) that markers of endoplasmic reticulum (BiP), intermediate compartment, and Golgi complex (rab1, CTR433, TGN38) label subsets of these subsynaptic organelles. Therefore, these findings indicate that synapses are equipped with the essential elements required for the synthesis and insertion of a well folded and glycosylated transmembrane protein.