Polarized sorting of glypiated proteins in hippocampal neurons

Abstract

OUR recent studies suggested that neurons and epithelial cells sort viral glycoproteins in a similar manner. The apical influenza virus haemagglutinin was preferentially delivered to the axon of hippocampal neurons in culture, whereas the basolateral vesicular stomatitis virus glycoprotein was sorted to the dendrites.¹ To investigate whether other membrane proteins showed similar sorting in neurons and epithelial cells, we have analysed the localization of a glypiated (glycosylphosphatidylinositol-anchored) protein, Thy-1, in hippocampal neurons in culture. In MDCK and other epithelial cells, endogenous glycosylphosphatidylinositol (GPI)-anchored proteins, as well as mutated exogenous proteins containing the GPI-attachment signal, undergo preferential delivery to the apical surface^2–4. This polarized sorting of GPI-anchored proteins has been proposed to occur by the same mechanisms as the sorting of glycolipids to the apical surface^5,6. We report here that the neuronal GPI-protein Thy-1 is present in hippocampal neurons in culture and is exclusively located on the axonal surface. This finding further strengthens our hypothesis that the mechanisms of sorting of surface components may be similar in neurons and epithelial cells.