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Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism

The B chain of ricin was expressed and delivered to the endoplasmic reticulum of tobacco protoplasts where it disappeared with time in a manner consistent with degradation. This turnover did not occur in the vacuoles or upon secretion. Indeed, several lines of evidence indicate that, in contrast to...

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Autores principales: Chamberlain, Kerry L., Marshall, Richard S., Jolliffe, Nicholas A., Frigerio, Lorenzo, Ceriotti, Aldo, Lord, J. Michael, Roberts, Lynne M.
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2586253/
https://www.ncbi.nlm.nih.gov/pubmed/18832379
http://dx.doi.org/10.1074/jbc.M805222200
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author Chamberlain, Kerry L.
Marshall, Richard S.
Jolliffe, Nicholas A.
Frigerio, Lorenzo
Ceriotti, Aldo
Lord, J. Michael
Roberts, Lynne M.
author_facet Chamberlain, Kerry L.
Marshall, Richard S.
Jolliffe, Nicholas A.
Frigerio, Lorenzo
Ceriotti, Aldo
Lord, J. Michael
Roberts, Lynne M.
author_sort Chamberlain, Kerry L.
collection PubMed
description The B chain of ricin was expressed and delivered to the endoplasmic reticulum of tobacco protoplasts where it disappeared with time in a manner consistent with degradation. This turnover did not occur in the vacuoles or upon secretion. Indeed, several lines of evidence indicate that, in contrast to the turnover of endoplasmic reticulum-targeted ricin A chain in the cytosol, the bulk of expressed ricin B chain was degraded in the secretory pathway.
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spelling pubmed-25862532008-12-03 Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism Chamberlain, Kerry L. Marshall, Richard S. Jolliffe, Nicholas A. Frigerio, Lorenzo Ceriotti, Aldo Lord, J. Michael Roberts, Lynne M. J Biol Chem Protein Synthesis, Post-Translational Modification, and Degradation The B chain of ricin was expressed and delivered to the endoplasmic reticulum of tobacco protoplasts where it disappeared with time in a manner consistent with degradation. This turnover did not occur in the vacuoles or upon secretion. Indeed, several lines of evidence indicate that, in contrast to the turnover of endoplasmic reticulum-targeted ricin A chain in the cytosol, the bulk of expressed ricin B chain was degraded in the secretory pathway. American Society for Biochemistry and Molecular Biology 2008-11-28 /pmc/articles/PMC2586253/ /pubmed/18832379 http://dx.doi.org/10.1074/jbc.M805222200 Text en Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Protein Synthesis, Post-Translational Modification, and Degradation
Chamberlain, Kerry L.
Marshall, Richard S.
Jolliffe, Nicholas A.
Frigerio, Lorenzo
Ceriotti, Aldo
Lord, J. Michael
Roberts, Lynne M.
Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title_full Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title_fullStr Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title_full_unstemmed Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title_short Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
title_sort ricin b chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a cdc48- and vacuole-independent mechanism
topic Protein Synthesis, Post-Translational Modification, and Degradation
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2586253/
https://www.ncbi.nlm.nih.gov/pubmed/18832379
http://dx.doi.org/10.1074/jbc.M805222200
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