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Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors
The coat protein II (COPII)–coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or wi...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4085702/ https://www.ncbi.nlm.nih.gov/pubmed/25002678 http://dx.doi.org/10.1083/jcb.201405020 |
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author | Kunduri, Govind Yuan, Changqing Parthibane, Velayoudame Nyswaner, Katherine M. Kanwar, Ritu Nagashima, Kunio Britt, Steven G. Mehta, Nickita Kotu, Varshika Porterfield, Mindy Tiemeyer, Michael Dolph, Patrick J. Acharya, Usha Acharya, Jairaj K. |
author_facet | Kunduri, Govind Yuan, Changqing Parthibane, Velayoudame Nyswaner, Katherine M. Kanwar, Ritu Nagashima, Kunio Britt, Steven G. Mehta, Nickita Kotu, Varshika Porterfield, Mindy Tiemeyer, Michael Dolph, Patrick J. Acharya, Usha Acharya, Jairaj K. |
author_sort | Kunduri, Govind |
collection | PubMed |
description | The coat protein II (COPII)–coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or with cargo receptors for anterograde trafficking. We show that cytosolic phosphatidic acid phospholipase A1 (PAPLA1) interacts with COPII protein family members and is required for the transport of Rh1 (rhodopsin 1), an N-glycosylated G protein–coupled receptor (GPCR), from the ER to the Golgi complex. In papla1 mutants, in the absence of transport to the Golgi, Rh1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected. Our findings show that a cytosolic protein is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking. |
format | Online Article Text |
id | pubmed-4085702 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-40857022015-01-07 Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors Kunduri, Govind Yuan, Changqing Parthibane, Velayoudame Nyswaner, Katherine M. Kanwar, Ritu Nagashima, Kunio Britt, Steven G. Mehta, Nickita Kotu, Varshika Porterfield, Mindy Tiemeyer, Michael Dolph, Patrick J. Acharya, Usha Acharya, Jairaj K. J Cell Biol Research Articles The coat protein II (COPII)–coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or with cargo receptors for anterograde trafficking. We show that cytosolic phosphatidic acid phospholipase A1 (PAPLA1) interacts with COPII protein family members and is required for the transport of Rh1 (rhodopsin 1), an N-glycosylated G protein–coupled receptor (GPCR), from the ER to the Golgi complex. In papla1 mutants, in the absence of transport to the Golgi, Rh1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected. Our findings show that a cytosolic protein is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking. The Rockefeller University Press 2014-07-07 /pmc/articles/PMC4085702/ /pubmed/25002678 http://dx.doi.org/10.1083/jcb.201405020 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Kunduri, Govind Yuan, Changqing Parthibane, Velayoudame Nyswaner, Katherine M. Kanwar, Ritu Nagashima, Kunio Britt, Steven G. Mehta, Nickita Kotu, Varshika Porterfield, Mindy Tiemeyer, Michael Dolph, Patrick J. Acharya, Usha Acharya, Jairaj K. Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title | Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title_full | Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title_fullStr | Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title_full_unstemmed | Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title_short | Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors |
title_sort | phosphatidic acid phospholipase a1 mediates er–golgi transit of a family of g protein–coupled receptors |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4085702/ https://www.ncbi.nlm.nih.gov/pubmed/25002678 http://dx.doi.org/10.1083/jcb.201405020 |
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