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Thy-1 expresses two signals for apical localization in epithelial cells
S K Powell1, M P Lisanti, E J Rodriguez-Boulan
1Department of Cell Biology and Anatomy, Cornell University Medical College, New York, New York 10021.
Recent work has shown that anchoring via glycosyl phosphatidylinositol (GPI) results in apical targeting for a variety of endogenous and transfected plasma membrane proteins expressed in epithelial cells. To further determine the correlation between GPI anchoring and apical localization, we expressed GPI-anchored and secretory forms of Thy-1 in Madin-Darby canine kidney cells by transfection. Native GPI-anchored Thy-1, normally expressed in thymocytes and neurons, was localized to the apical surface. A truncated form of Thy-1, lacking 22 out of 31 hydrophobic amino acids at the COOH-terminus, was also constructed; this deletion blocked attachment of the GPI anchor and resulted in apical secretion of Thy-1. In combination with previous results, our observations indicate that Thy-1 contains apical targeting information in its protein sequence as well as in the GPI anchor.
Recent work has shown that anchoring via glycosyl phosphatidylinositol (GPI) results in apical targeting for a variety of endogenous and transfected plasma membrane proteins expressed in epithelial cells. To further determine the correlation between GPI anchoring and apical localization, we expressed GPI-anchored and secretory forms of Thy-1 in Madin-Darby canine kidney cells by transfection. Native GPI-anchored Thy-1, normally expressed in thymocytes and neurons, was localized to the apical surface. A truncated form of Thy-1, lacking 22 out of 31 hydrophobic amino acids at the COOH-terminus, was also constructed; this deletion blocked attachment of the GPI anchor and resulted in apical secretion of Thy-1. In combination with previous results, our observations indicate that Thy-1 contains apical targeting information in its protein sequence as well as in the GPI anchor.