The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network

The membrane-spanning and cytoplasmic domains of CD4 and CD8 were replaced by those of TGN38. After transient expression in HeLa cells, the location of the hybrid proteins was determined using immunofluorescence and quantitative immuno-electron microscopy, FACS analysis and metabolic labeling. The m...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1994
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120028/
https://www.ncbi.nlm.nih.gov/pubmed/8163544
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description The membrane-spanning and cytoplasmic domains of CD4 and CD8 were replaced by those of TGN38. After transient expression in HeLa cells, the location of the hybrid proteins was determined using immunofluorescence and quantitative immuno-electron microscopy, FACS analysis and metabolic labeling. The membrane-spanning domain was found to contain a signal that localized hybrid proteins to the TGN. This was in addition to the signal previously identified in the cytoplasmic domain (Bos, K., C. Wraight, and K. Stanley. 1993. EMBO (Eur. Mol. Biol. Organ) J. 12:2219-2228. Humphrey, J. S., P. J. Peters, L. C. Yuan, and J. S. Bonifacino. 1993. J. Cell Biol. 120:1123-1135. Wong, S. H., and W. Hong. 1993. J. Biol. Chem. 268:22853-22862). The different properties of these two signals suggest that each operates by a different mechanism.
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spelling pubmed-21200282008-05-01 The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network J Cell Biol Articles The membrane-spanning and cytoplasmic domains of CD4 and CD8 were replaced by those of TGN38. After transient expression in HeLa cells, the location of the hybrid proteins was determined using immunofluorescence and quantitative immuno-electron microscopy, FACS analysis and metabolic labeling. The membrane-spanning domain was found to contain a signal that localized hybrid proteins to the TGN. This was in addition to the signal previously identified in the cytoplasmic domain (Bos, K., C. Wraight, and K. Stanley. 1993. EMBO (Eur. Mol. Biol. Organ) J. 12:2219-2228. Humphrey, J. S., P. J. Peters, L. C. Yuan, and J. S. Bonifacino. 1993. J. Cell Biol. 120:1123-1135. Wong, S. H., and W. Hong. 1993. J. Biol. Chem. 268:22853-22862). The different properties of these two signals suggest that each operates by a different mechanism. The Rockefeller University Press 1994-04-02 /pmc/articles/PMC2120028/ /pubmed/8163544 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title_full The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title_fullStr The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title_full_unstemmed The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title_short The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
title_sort tgn38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-golgi network
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120028/
https://www.ncbi.nlm.nih.gov/pubmed/8163544

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