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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Autores principales: A. Manuel Liaci, Friedrich Förster
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Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/7809aa2c4b524298afeb574ef8141eda
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spelling oai:doaj.org-article:7809aa2c4b524298afeb574ef8141eda2021-11-11T17:17:37ZTake Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation10.3390/ijms2221118711422-00671661-6596https://doaj.org/article/7809aa2c4b524298afeb574ef8141eda2021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11871https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Cleavable 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.A. Manuel LiaciFriedrich FörsterMDPI AGarticlesignal peptidesignal peptidaseER transloconendoplasmic reticulumprotein targetingchaperonesBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11871, p 11871 (2021)
institution DOAJ
collection DOAJ
language EN
topic signal peptide
signal peptidase
ER translocon
endoplasmic reticulum
protein targeting
chaperones
Biology (General)
QH301-705.5
Chemistry
QD1-999
spellingShingle signal peptide
signal peptidase
ER translocon
endoplasmic reticulum
protein targeting
chaperones
Biology (General)
QH301-705.5
Chemistry
QD1-999
A. Manuel Liaci
Friedrich Förster
Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
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.
format article
author A. Manuel Liaci
Friedrich Förster
author_facet A. Manuel Liaci
Friedrich Förster
author_sort A. Manuel Liaci
title 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_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_sort take me home, protein roads: structural insights into signal peptide interactions during er translocation
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/7809aa2c4b524298afeb574ef8141eda
work_keys_str_mv AT amanuelliaci takemehomeproteinroadsstructuralinsightsintosignalpeptideinteractionsduringertranslocation
AT friedrichforster takemehomeproteinroadsstructuralinsightsintosignalpeptideinteractionsduringertranslocation
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