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Understanding the mammalian TRAP complex function(s)

In eukaryotic cells, about one-third of the synthesized proteins are translocated into the endoplasmic reticulum; they are membrane or lumen resident proteins and proteins direct to the Golgi apparatus. The co-translational translocation takes place through the heterotrimeric protein-conducting chan...

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Autor principal: Russo, Antonietta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7276530/
https://www.ncbi.nlm.nih.gov/pubmed/32453970
http://dx.doi.org/10.1098/rsob.190244
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author Russo, Antonietta
author_facet Russo, Antonietta
author_sort Russo, Antonietta
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description In eukaryotic cells, about one-third of the synthesized proteins are translocated into the endoplasmic reticulum; they are membrane or lumen resident proteins and proteins direct to the Golgi apparatus. The co-translational translocation takes place through the heterotrimeric protein-conducting channel Sec61 which is associated with the ribosome and many accessory components, such as the heterotetrameric translocon-associated protein (TRAP) complex. Recently, microscopic techniques, such as cryo-electron microscopy and cryo-electron tomography, have enabled the determination of the translocation machinery structure. However, at present, there is a lack of understanding regarding the roles of some of its components; indeed, the TRAP complex function during co-translational translocation needs to be established. In addition, TRAP may play a role during unfolded protein response, endoplasmic-reticulum-associated protein degradation and congenital disorder of glycosylation (ssr4 CDG). In this article, I describe the current understanding of the TRAP complex in the light of its possible function(s).
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spelling pubmed-72765302020-06-08 Understanding the mammalian TRAP complex function(s) Russo, Antonietta Open Biol Review In eukaryotic cells, about one-third of the synthesized proteins are translocated into the endoplasmic reticulum; they are membrane or lumen resident proteins and proteins direct to the Golgi apparatus. The co-translational translocation takes place through the heterotrimeric protein-conducting channel Sec61 which is associated with the ribosome and many accessory components, such as the heterotetrameric translocon-associated protein (TRAP) complex. Recently, microscopic techniques, such as cryo-electron microscopy and cryo-electron tomography, have enabled the determination of the translocation machinery structure. However, at present, there is a lack of understanding regarding the roles of some of its components; indeed, the TRAP complex function during co-translational translocation needs to be established. In addition, TRAP may play a role during unfolded protein response, endoplasmic-reticulum-associated protein degradation and congenital disorder of glycosylation (ssr4 CDG). In this article, I describe the current understanding of the TRAP complex in the light of its possible function(s). The Royal Society 2020-05-27 /pmc/articles/PMC7276530/ /pubmed/32453970 http://dx.doi.org/10.1098/rsob.190244 Text en © 2020 The Authors. http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Review
Russo, Antonietta
Understanding the mammalian TRAP complex function(s)
title Understanding the mammalian TRAP complex function(s)
title_full Understanding the mammalian TRAP complex function(s)
title_fullStr Understanding the mammalian TRAP complex function(s)
title_full_unstemmed Understanding the mammalian TRAP complex function(s)
title_short Understanding the mammalian TRAP complex function(s)
title_sort understanding the mammalian trap complex function(s)
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7276530/
https://www.ncbi.nlm.nih.gov/pubmed/32453970
http://dx.doi.org/10.1098/rsob.190244
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