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Membrane biogenesis and the unfolded protein response
In addition to serving as the entry point for newly translated polypeptides making their way through the secretory pathway, the endoplasmic reticulum (ER) also synthesizes many lipid components of the entire endomembrane system. A report published in this issue implicates a signaling pathway known t...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2004
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172515/ https://www.ncbi.nlm.nih.gov/pubmed/15479733 http://dx.doi.org/10.1083/jcb.200408117 |
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author | Ron, David Hampton, Randolph Y. |
author_facet | Ron, David Hampton, Randolph Y. |
author_sort | Ron, David |
collection | PubMed |
description | In addition to serving as the entry point for newly translated polypeptides making their way through the secretory pathway, the endoplasmic reticulum (ER) also synthesizes many lipid components of the entire endomembrane system. A report published in this issue implicates a signaling pathway known to respond to ER unfolded protein load in the control of phospholipid biosynthesis by the organelle (Sriburi et al., 2004). The reasonable notion that demand for ER membrane is integrated with protein processing capacity was initially suggested by genetic analysis of yeast. The new data lend direct support for this idea and imply interesting mechanistic possibilities for how this coupling develops. |
format | Text |
id | pubmed-2172515 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21725152008-03-05 Membrane biogenesis and the unfolded protein response Ron, David Hampton, Randolph Y. J Cell Biol Reviews In addition to serving as the entry point for newly translated polypeptides making their way through the secretory pathway, the endoplasmic reticulum (ER) also synthesizes many lipid components of the entire endomembrane system. A report published in this issue implicates a signaling pathway known to respond to ER unfolded protein load in the control of phospholipid biosynthesis by the organelle (Sriburi et al., 2004). The reasonable notion that demand for ER membrane is integrated with protein processing capacity was initially suggested by genetic analysis of yeast. The new data lend direct support for this idea and imply interesting mechanistic possibilities for how this coupling develops. The Rockefeller University Press 2004-10-11 /pmc/articles/PMC2172515/ /pubmed/15479733 http://dx.doi.org/10.1083/jcb.200408117 Text en Copyright © 2004, 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 | Reviews Ron, David Hampton, Randolph Y. Membrane biogenesis and the unfolded protein response |
title | Membrane biogenesis and the unfolded protein response |
title_full | Membrane biogenesis and the unfolded protein response |
title_fullStr | Membrane biogenesis and the unfolded protein response |
title_full_unstemmed | Membrane biogenesis and the unfolded protein response |
title_short | Membrane biogenesis and the unfolded protein response |
title_sort | membrane biogenesis and the unfolded protein response |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172515/ https://www.ncbi.nlm.nih.gov/pubmed/15479733 http://dx.doi.org/10.1083/jcb.200408117 |
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