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Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal
Although numerous linear motifs that direct protein trafficking within cells have been identified, there are few examples of linear sorting signals mediating directed export of membrane proteins from the Golgi complex to the plasma membrane. The reovirus fusion-associated small transmembrane protein...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952855/ https://www.ncbi.nlm.nih.gov/pubmed/24451258 http://dx.doi.org/10.1091/mbc.E13-07-0364 |
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author | Parmar, Hirendrasinh B. Barry, Christopher Kai, FuiBoon Duncan, Roy |
author_facet | Parmar, Hirendrasinh B. Barry, Christopher Kai, FuiBoon Duncan, Roy |
author_sort | Parmar, Hirendrasinh B. |
collection | PubMed |
description | Although numerous linear motifs that direct protein trafficking within cells have been identified, there are few examples of linear sorting signals mediating directed export of membrane proteins from the Golgi complex to the plasma membrane. The reovirus fusion-associated small transmembrane proteins are simple, single-pass transmembrane proteins that traffic through the endoplasmic reticulum–Golgi pathway to the plasma membrane, where they induce cell–cell membrane fusion. Here we show that a membrane-proximal, polybasic motif (PBM) in the cytosolic tail of p14 is essential for efficient export of p14 from the Golgi complex to the plasma membrane. Extensive mutagenic analysis reveals that the number, but not the identity or position, of basic residues present in the PBM dictates p14 export from the Golgi complex, with a minimum of three basic residues required for efficient Golgi export. Results further indicate that the tribasic motif does not affect plasma membrane retention of p14. Furthermore, introduction of the tribasic motif into a Golgi-localized, chimeric ERGIC-53 protein directs export from the Golgi complex to the plasma membrane. The p14 PBM is the first example of an autonomous, tribasic signal required for Golgi export to the plasma membrane. |
format | Online Article Text |
id | pubmed-3952855 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-39528552014-05-30 Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal Parmar, Hirendrasinh B. Barry, Christopher Kai, FuiBoon Duncan, Roy Mol Biol Cell Articles Although numerous linear motifs that direct protein trafficking within cells have been identified, there are few examples of linear sorting signals mediating directed export of membrane proteins from the Golgi complex to the plasma membrane. The reovirus fusion-associated small transmembrane proteins are simple, single-pass transmembrane proteins that traffic through the endoplasmic reticulum–Golgi pathway to the plasma membrane, where they induce cell–cell membrane fusion. Here we show that a membrane-proximal, polybasic motif (PBM) in the cytosolic tail of p14 is essential for efficient export of p14 from the Golgi complex to the plasma membrane. Extensive mutagenic analysis reveals that the number, but not the identity or position, of basic residues present in the PBM dictates p14 export from the Golgi complex, with a minimum of three basic residues required for efficient Golgi export. Results further indicate that the tribasic motif does not affect plasma membrane retention of p14. Furthermore, introduction of the tribasic motif into a Golgi-localized, chimeric ERGIC-53 protein directs export from the Golgi complex to the plasma membrane. The p14 PBM is the first example of an autonomous, tribasic signal required for Golgi export to the plasma membrane. The American Society for Cell Biology 2014-03-15 /pmc/articles/PMC3952855/ /pubmed/24451258 http://dx.doi.org/10.1091/mbc.E13-07-0364 Text en © 2014 Parmar et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Parmar, Hirendrasinh B. Barry, Christopher Kai, FuiBoon Duncan, Roy Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title | Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title_full | Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title_fullStr | Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title_full_unstemmed | Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title_short | Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal |
title_sort | golgi complex–plasma membrane trafficking directed by an autonomous, tribasic golgi export signal |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952855/ https://www.ncbi.nlm.nih.gov/pubmed/24451258 http://dx.doi.org/10.1091/mbc.E13-07-0364 |
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