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Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation

Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable signal sequences target roughly a quarter of the human proteome to the ER. These short peptides, mostly located at the N-termini of proteins, are highly diverse. For most proteins targeted to the ER, it is the interac...

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Detalles Bibliográficos
Autores principales: Liaci, A. Manuel, Förster, Friedrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8584900/
https://www.ncbi.nlm.nih.gov/pubmed/34769302
http://dx.doi.org/10.3390/ijms222111871
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author Liaci, A. Manuel
Förster, Friedrich
author_facet Liaci, A. Manuel
Förster, Friedrich
author_sort Liaci, A. Manuel
collection PubMed
description Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable signal sequences target roughly a quarter of the human proteome to the ER. These short peptides, mostly located at the N-termini of proteins, are highly diverse. For most proteins targeted to the ER, it is the interactions between the signal sequences and the various ER targeting and translocation machineries such as the signal recognition particle (SRP), the protein-conducting channel Sec61, and the signal peptidase complex (SPC) that determine the proteins’ target location and provide translocation fidelity. In this review, we follow the signal peptide into the ER and discuss the recent insights that structural biology has provided on the governing principles of those interactions.
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spelling pubmed-85849002021-11-12 Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation Liaci, A. Manuel Förster, Friedrich Int J Mol Sci Review Cleavable endoplasmic reticulum (ER) signal peptides (SPs) and other non-cleavable signal sequences target roughly a quarter of the human proteome to the ER. These short peptides, mostly located at the N-termini of proteins, are highly diverse. For most proteins targeted to the ER, it is the interactions between the signal sequences and the various ER targeting and translocation machineries such as the signal recognition particle (SRP), the protein-conducting channel Sec61, and the signal peptidase complex (SPC) that determine the proteins’ target location and provide translocation fidelity. In this review, we follow the signal peptide into the ER and discuss the recent insights that structural biology has provided on the governing principles of those interactions. MDPI 2021-11-01 /pmc/articles/PMC8584900/ /pubmed/34769302 http://dx.doi.org/10.3390/ijms222111871 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Liaci, A. Manuel
Förster, Friedrich
Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title_full Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title_fullStr Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title_full_unstemmed Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title_short Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
title_sort take me home, protein roads: structural insights into signal peptide interactions during er translocation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8584900/
https://www.ncbi.nlm.nih.gov/pubmed/34769302
http://dx.doi.org/10.3390/ijms222111871
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AT forsterfriedrich takemehomeproteinroadsstructuralinsightsintosignalpeptideinteractionsduringertranslocation