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Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells
Polarized exocytosis plays a major role in development and cell differentiation but the mechanisms that target exocytosis to specific membrane domains in animal cells are still poorly understood. We characterized Drosophila Sec6, a component of the exocyst complex that is believed to tether secretor...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171699/ https://www.ncbi.nlm.nih.gov/pubmed/15897260 http://dx.doi.org/10.1083/jcb.200410081 |
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author | Beronja, Slobodan Laprise, Patrick Papoulas, Ophelia Pellikka, Milena Sisson, John Tepass, Ulrich |
author_facet | Beronja, Slobodan Laprise, Patrick Papoulas, Ophelia Pellikka, Milena Sisson, John Tepass, Ulrich |
author_sort | Beronja, Slobodan |
collection | PubMed |
description | Polarized exocytosis plays a major role in development and cell differentiation but the mechanisms that target exocytosis to specific membrane domains in animal cells are still poorly understood. We characterized Drosophila Sec6, a component of the exocyst complex that is believed to tether secretory vesicles to specific plasma membrane sites. sec6 mutations cause cell lethality and disrupt plasma membrane growth. In developing photoreceptor cells (PRCs), Sec6 but not Sec5 or Sec8 shows accumulation at adherens junctions. In late PRCs, Sec6, Sec5, and Sec8 colocalize at the rhabdomere, the light sensing subdomain of the apical membrane. PRCs with reduced Sec6 function accumulate secretory vesicles and fail to transport proteins to the rhabdomere, but show normal localization of proteins to the apical stalk membrane and the basolateral membrane. Furthermore, we show that Rab11 forms a complex with Sec5 and that Sec5 interacts with Sec6 suggesting that the exocyst is a Rab11 effector that facilitates protein transport to the apical rhabdomere in Drosophila PRCs. |
format | Text |
id | pubmed-2171699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21716992008-03-05 Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells Beronja, Slobodan Laprise, Patrick Papoulas, Ophelia Pellikka, Milena Sisson, John Tepass, Ulrich J Cell Biol Research Articles Polarized exocytosis plays a major role in development and cell differentiation but the mechanisms that target exocytosis to specific membrane domains in animal cells are still poorly understood. We characterized Drosophila Sec6, a component of the exocyst complex that is believed to tether secretory vesicles to specific plasma membrane sites. sec6 mutations cause cell lethality and disrupt plasma membrane growth. In developing photoreceptor cells (PRCs), Sec6 but not Sec5 or Sec8 shows accumulation at adherens junctions. In late PRCs, Sec6, Sec5, and Sec8 colocalize at the rhabdomere, the light sensing subdomain of the apical membrane. PRCs with reduced Sec6 function accumulate secretory vesicles and fail to transport proteins to the rhabdomere, but show normal localization of proteins to the apical stalk membrane and the basolateral membrane. Furthermore, we show that Rab11 forms a complex with Sec5 and that Sec5 interacts with Sec6 suggesting that the exocyst is a Rab11 effector that facilitates protein transport to the apical rhabdomere in Drosophila PRCs. The Rockefeller University Press 2005-05-23 /pmc/articles/PMC2171699/ /pubmed/15897260 http://dx.doi.org/10.1083/jcb.200410081 Text en Copyright © 2005, The Rockefeller University Press 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 | Research Articles Beronja, Slobodan Laprise, Patrick Papoulas, Ophelia Pellikka, Milena Sisson, John Tepass, Ulrich Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title | Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title_full | Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title_fullStr | Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title_full_unstemmed | Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title_short | Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells |
title_sort | essential function of drosophila sec6 in apical exocytosis of epithelial photoreceptor cells |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171699/ https://www.ncbi.nlm.nih.gov/pubmed/15897260 http://dx.doi.org/10.1083/jcb.200410081 |
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