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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...

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Detalles Bibliográficos
Autores principales: Jiang, Liwen, Phillips, Thomas E., Rogers, Sally W., Rogers, John C.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
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.
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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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