Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
AUTOR(ES)
Puddington, L
RESUMO
The envelope glycoprotein (G protein) of vesicular stomatitis virus (VSV) is transported to the basolateral plasma membrane of polarized epithelial cells, whereas the hemagglutinin glycoprotein (HA protein) of influenza virus is transported to the apical plasma membrane. To determine if the cytoplasmic domain of VSV G protein might be important in directing G protein to the basolateral membrane, we derived polarized Madin-Darby canine kidney cell lines expressing G protein or G protein with its normal cytoplasmic domain replaced with the cytoplasmic domain from an influenza HA protein (GHA protein). Indirect immunofluorescence microscopy showed that G protein was present primarily on basolateral surfaces, whereas the GHA protein was present on the apical and basolateral membranes. These results suggest that the cytoplasmic domain can be an important determinant directing polarized expression of an integral membrane protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=304737Documentos Relacionados
- Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.
- The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells.
- The Viral Spike Protein Is Not Involved in the Polarized Sorting of Coronaviruses in Epithelial Cells†
- Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.
- Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain.