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Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum
The length and hydrophobicity of the transmembrane domain (TMD) play an important role in the sorting of membrane proteins within the secretory pathway; however, the relative contributions of protein–protein and protein–lipid interactions to this phenomenon are currently not understood. To investiga...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287291/ https://www.ncbi.nlm.nih.gov/pubmed/18391072 http://dx.doi.org/10.1083/jcb.200710093 |
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author | Ronchi, Paolo Colombo, Sara Francolini, Maura Borgese, Nica |
author_facet | Ronchi, Paolo Colombo, Sara Francolini, Maura Borgese, Nica |
author_sort | Ronchi, Paolo |
collection | PubMed |
description | The length and hydrophobicity of the transmembrane domain (TMD) play an important role in the sorting of membrane proteins within the secretory pathway; however, the relative contributions of protein–protein and protein–lipid interactions to this phenomenon are currently not understood. To investigate the mechanism of TMD-dependent sorting, we used the following two C tail–anchored fluorescent proteins (FPs), which differ only in TMD length: FP-17, which is anchored to the endoplasmic reticulum (ER) membrane by 17 uncharged residues, and FP-22, which is driven to the plasma membrane by its 22-residue-long TMD. Before export of FP-22, the two constructs, although freely diffusible, were seen to distribute differently between ER tubules and sheets. Analyses in temperature-blocked cells revealed that FP-17 is excluded from ER exit sites, whereas FP-22 is recruited to them, although it remains freely exchangeable with the surrounding reticulum. Thus, physicochemical features of the TMD influence sorting of membrane proteins both within the ER and at the ER–Golgi boundary by simple receptor-independent mechanisms based on partitioning. |
format | Text |
id | pubmed-2287291 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22872912008-10-07 Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum Ronchi, Paolo Colombo, Sara Francolini, Maura Borgese, Nica J Cell Biol Research Articles The length and hydrophobicity of the transmembrane domain (TMD) play an important role in the sorting of membrane proteins within the secretory pathway; however, the relative contributions of protein–protein and protein–lipid interactions to this phenomenon are currently not understood. To investigate the mechanism of TMD-dependent sorting, we used the following two C tail–anchored fluorescent proteins (FPs), which differ only in TMD length: FP-17, which is anchored to the endoplasmic reticulum (ER) membrane by 17 uncharged residues, and FP-22, which is driven to the plasma membrane by its 22-residue-long TMD. Before export of FP-22, the two constructs, although freely diffusible, were seen to distribute differently between ER tubules and sheets. Analyses in temperature-blocked cells revealed that FP-17 is excluded from ER exit sites, whereas FP-22 is recruited to them, although it remains freely exchangeable with the surrounding reticulum. Thus, physicochemical features of the TMD influence sorting of membrane proteins both within the ER and at the ER–Golgi boundary by simple receptor-independent mechanisms based on partitioning. The Rockefeller University Press 2008-04-07 /pmc/articles/PMC2287291/ /pubmed/18391072 http://dx.doi.org/10.1083/jcb.200710093 Text en Copyright © 2008, 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 | Research Articles Ronchi, Paolo Colombo, Sara Francolini, Maura Borgese, Nica Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title | Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title_full | Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title_fullStr | Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title_full_unstemmed | Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title_short | Transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
title_sort | transmembrane domain–dependent partitioning of membrane proteins within the endoplasmic reticulum |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2287291/ https://www.ncbi.nlm.nih.gov/pubmed/18391072 http://dx.doi.org/10.1083/jcb.200710093 |
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