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Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements

Essentially all cellular processes are orchestrated by protein-protein interactions (PPIs). In recent years, affinity purification coupled to mass spectrometry (AP-MS) has been the preferred method to identify cellular PPIs. Here we present a microfluidic-based AP-MS workflow, called on-chip AP-MS,...

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Autores principales: Furlan, Cristina, Dirks, René A. M., Thomas, Peter C., Jones, Robert C., Wang, Jing, Lynch, Mark, Marks, Hendrik, Vermeulen, Michiel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6449397/
https://www.ncbi.nlm.nih.gov/pubmed/30948724
http://dx.doi.org/10.1038/s41467-019-09533-y
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author Furlan, Cristina
Dirks, René A. M.
Thomas, Peter C.
Jones, Robert C.
Wang, Jing
Lynch, Mark
Marks, Hendrik
Vermeulen, Michiel
author_facet Furlan, Cristina
Dirks, René A. M.
Thomas, Peter C.
Jones, Robert C.
Wang, Jing
Lynch, Mark
Marks, Hendrik
Vermeulen, Michiel
author_sort Furlan, Cristina
collection PubMed
description Essentially all cellular processes are orchestrated by protein-protein interactions (PPIs). In recent years, affinity purification coupled to mass spectrometry (AP-MS) has been the preferred method to identify cellular PPIs. Here we present a microfluidic-based AP-MS workflow, called on-chip AP-MS, to identify PPIs using minute amounts of input material. By using this automated platform we purify the human Cohesin, CCC and Mediator complexes from as little as 4 micrograms of input lysate, representing a 50─100-fold downscaling compared to regular microcentrifuge tube-based protocols. We show that our platform can be used to affinity purify tagged baits as well as native cellular proteins and their interaction partners. As such, our method holds great promise for future biological and clinical AP-MS applications in which sample amounts are limited.
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spelling pubmed-64493972019-04-08 Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements Furlan, Cristina Dirks, René A. M. Thomas, Peter C. Jones, Robert C. Wang, Jing Lynch, Mark Marks, Hendrik Vermeulen, Michiel Nat Commun Article Essentially all cellular processes are orchestrated by protein-protein interactions (PPIs). In recent years, affinity purification coupled to mass spectrometry (AP-MS) has been the preferred method to identify cellular PPIs. Here we present a microfluidic-based AP-MS workflow, called on-chip AP-MS, to identify PPIs using minute amounts of input material. By using this automated platform we purify the human Cohesin, CCC and Mediator complexes from as little as 4 micrograms of input lysate, representing a 50─100-fold downscaling compared to regular microcentrifuge tube-based protocols. We show that our platform can be used to affinity purify tagged baits as well as native cellular proteins and their interaction partners. As such, our method holds great promise for future biological and clinical AP-MS applications in which sample amounts are limited. Nature Publishing Group UK 2019-04-04 /pmc/articles/PMC6449397/ /pubmed/30948724 http://dx.doi.org/10.1038/s41467-019-09533-y Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Furlan, Cristina
Dirks, René A. M.
Thomas, Peter C.
Jones, Robert C.
Wang, Jing
Lynch, Mark
Marks, Hendrik
Vermeulen, Michiel
Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title_full Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title_fullStr Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title_full_unstemmed Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title_short Miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
title_sort miniaturised interaction proteomics on a microfluidic platform with ultra-low input requirements
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6449397/
https://www.ncbi.nlm.nih.gov/pubmed/30948724
http://dx.doi.org/10.1038/s41467-019-09533-y
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