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Golgi retention signals: do membranes hold the key?

The diverse forms and functions of cellular organelles are, presumably, a consequence of their particular molecular compositions. The generation and maintenance of this diversity is achieved by the targeting of newly synthesized proteins to specific locations and their subsequent retention there. Se...

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Detalles Bibliográficos
Autor principal: Machamer, Carolyn E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Ltd. 1991
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7135602/
https://www.ncbi.nlm.nih.gov/pubmed/14731855
http://dx.doi.org/10.1016/0962-8924(91)90001-P
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author Machamer, Carolyn E.
author_facet Machamer, Carolyn E.
author_sort Machamer, Carolyn E.
collection PubMed
description The diverse forms and functions of cellular organelles are, presumably, a consequence of their particular molecular compositions. The generation and maintenance of this diversity is achieved by the targeting of newly synthesized proteins to specific locations and their subsequent retention there. Sequences that retain proteins in the endoplasmic reticulum (ER) have been identified at the C-termini of resident ER proteins, where they are readily accessible to potential receptors. By contrast, recent results have demonstrated that retention of proteins in the Golgi complex involves sequences located within transmembrane domains. This suggests the novel possibility that the membrane composition of the Golgi complex plays a role in retention of resident Golgi proteins.
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spelling pubmed-71356022020-04-08 Golgi retention signals: do membranes hold the key? Machamer, Carolyn E. Trends Cell Biol Article The diverse forms and functions of cellular organelles are, presumably, a consequence of their particular molecular compositions. The generation and maintenance of this diversity is achieved by the targeting of newly synthesized proteins to specific locations and their subsequent retention there. Sequences that retain proteins in the endoplasmic reticulum (ER) have been identified at the C-termini of resident ER proteins, where they are readily accessible to potential receptors. By contrast, recent results have demonstrated that retention of proteins in the Golgi complex involves sequences located within transmembrane domains. This suggests the novel possibility that the membrane composition of the Golgi complex plays a role in retention of resident Golgi proteins. Published by Elsevier Ltd. 1991-12 2002-12-18 /pmc/articles/PMC7135602/ /pubmed/14731855 http://dx.doi.org/10.1016/0962-8924(91)90001-P Text en Copyright © 1991 Published by Elsevier Ltd. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Machamer, Carolyn E.
Golgi retention signals: do membranes hold the key?
title Golgi retention signals: do membranes hold the key?
title_full Golgi retention signals: do membranes hold the key?
title_fullStr Golgi retention signals: do membranes hold the key?
title_full_unstemmed Golgi retention signals: do membranes hold the key?
title_short Golgi retention signals: do membranes hold the key?
title_sort golgi retention signals: do membranes hold the key?
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7135602/
https://www.ncbi.nlm.nih.gov/pubmed/14731855
http://dx.doi.org/10.1016/0962-8924(91)90001-P
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