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Biogenesis of the Protein Storage Vacuole Crystalloid
We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a no...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2000
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175284/ https://www.ncbi.nlm.nih.gov/pubmed/10953001 |
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author | Jiang, Liwen Phillips, Thomas E. Rogers, Sally W. Rogers, John C. |
author_facet | Jiang, Liwen Phillips, Thomas E. Rogers, Sally W. Rogers, John C. |
author_sort | Jiang, Liwen |
collection | PubMed |
description | We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage. |
format | Text |
id | pubmed-2175284 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21752842008-05-01 Biogenesis of the Protein Storage Vacuole Crystalloid Jiang, Liwen Phillips, Thomas E. Rogers, Sally W. Rogers, John C. J Cell Biol Original Article We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage. The Rockefeller University Press 2000-08-21 /pmc/articles/PMC2175284/ /pubmed/10953001 Text en © 2000 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 | Original Article Jiang, Liwen Phillips, Thomas E. Rogers, Sally W. Rogers, John C. Biogenesis of the Protein Storage Vacuole Crystalloid |
title | Biogenesis of the Protein Storage Vacuole Crystalloid |
title_full | Biogenesis of the Protein Storage Vacuole Crystalloid |
title_fullStr | Biogenesis of the Protein Storage Vacuole Crystalloid |
title_full_unstemmed | Biogenesis of the Protein Storage Vacuole Crystalloid |
title_short | Biogenesis of the Protein Storage Vacuole Crystalloid |
title_sort | biogenesis of the protein storage vacuole crystalloid |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175284/ https://www.ncbi.nlm.nih.gov/pubmed/10953001 |
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