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Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion
For a long time, leaderless secreted proteins (LLSP) were neglected as artifacts derived from dying cells. It is now generally accepted that secretion of LLSP–as a part of the collective term unconventional protein secretion (UPS) - is an evolutionarily conserved process and that these LLSP are acti...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8980719/ https://www.ncbi.nlm.nih.gov/pubmed/35392176 http://dx.doi.org/10.3389/fcell.2022.878027 |
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author | Poschmann, Gereon Bahr, Jasmin Schrader, Jürgen Stejerean-Todoran, Ioana Bogeski, Ivan Stühler, Kai |
author_facet | Poschmann, Gereon Bahr, Jasmin Schrader, Jürgen Stejerean-Todoran, Ioana Bogeski, Ivan Stühler, Kai |
author_sort | Poschmann, Gereon |
collection | PubMed |
description | For a long time, leaderless secreted proteins (LLSP) were neglected as artifacts derived from dying cells. It is now generally accepted that secretion of LLSP–as a part of the collective term unconventional protein secretion (UPS) - is an evolutionarily conserved process and that these LLSP are actively and selectively secreted from living cells bypassing the classical endoplasmic reticulum-Golgi pathway. However, the mechanism of UPS pathways, as well as the number of LLSP and which part of a protein is involved in the selection of LLSPs for secretion, are still enigmatic and await clarification. Secretomics-a proteomics-based approach to identify and quantify all proteins secreted by a cell-is inherently unbiased toward a particular secretion pathway and offers the opportunity to shed light on the UPS. Here, we will evaluate and present recent results of proteomic workflows allowing to obtain high-confident secretome data. Additionally, we address that cell culture conditions largely affect the composition of the secretome. This has to be kept in mind to control cell culture induced artifacts and adaptation stress in serum free conditions. Evaluation of click chemistry for secretome analysis of cells under serum-containing conditions showed a significant change in the cellular proteome with longer incubation time upon treatment with non-canonical amino acid azidohomoalanine. Finally, we showed that the number of LLSP far exceeds the number of secreted proteins annotated in Uniprot and ProteinAtlas. Thus, secretomics in combination with sophisticated microbioanalytical and sample preparation methods is well suited to provide a comprehensive picture of UPS. |
format | Online Article Text |
id | pubmed-8980719 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-89807192022-04-06 Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion Poschmann, Gereon Bahr, Jasmin Schrader, Jürgen Stejerean-Todoran, Ioana Bogeski, Ivan Stühler, Kai Front Cell Dev Biol Cell and Developmental Biology For a long time, leaderless secreted proteins (LLSP) were neglected as artifacts derived from dying cells. It is now generally accepted that secretion of LLSP–as a part of the collective term unconventional protein secretion (UPS) - is an evolutionarily conserved process and that these LLSP are actively and selectively secreted from living cells bypassing the classical endoplasmic reticulum-Golgi pathway. However, the mechanism of UPS pathways, as well as the number of LLSP and which part of a protein is involved in the selection of LLSPs for secretion, are still enigmatic and await clarification. Secretomics-a proteomics-based approach to identify and quantify all proteins secreted by a cell-is inherently unbiased toward a particular secretion pathway and offers the opportunity to shed light on the UPS. Here, we will evaluate and present recent results of proteomic workflows allowing to obtain high-confident secretome data. Additionally, we address that cell culture conditions largely affect the composition of the secretome. This has to be kept in mind to control cell culture induced artifacts and adaptation stress in serum free conditions. Evaluation of click chemistry for secretome analysis of cells under serum-containing conditions showed a significant change in the cellular proteome with longer incubation time upon treatment with non-canonical amino acid azidohomoalanine. Finally, we showed that the number of LLSP far exceeds the number of secreted proteins annotated in Uniprot and ProteinAtlas. Thus, secretomics in combination with sophisticated microbioanalytical and sample preparation methods is well suited to provide a comprehensive picture of UPS. Frontiers Media S.A. 2022-03-22 /pmc/articles/PMC8980719/ /pubmed/35392176 http://dx.doi.org/10.3389/fcell.2022.878027 Text en Copyright © 2022 Poschmann, Bahr, Schrader, Stejerean-Todoran, Bogeski and Stühler. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cell and Developmental Biology Poschmann, Gereon Bahr, Jasmin Schrader, Jürgen Stejerean-Todoran, Ioana Bogeski, Ivan Stühler, Kai Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title | Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title_full | Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title_fullStr | Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title_full_unstemmed | Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title_short | Secretomics—A Key to a Comprehensive Picture of Unconventional Protein Secretion |
title_sort | secretomics—a key to a comprehensive picture of unconventional protein secretion |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8980719/ https://www.ncbi.nlm.nih.gov/pubmed/35392176 http://dx.doi.org/10.3389/fcell.2022.878027 |
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