A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions

Abstract Interactions between membrane proteins within a cellular environment are crucial for all living cells. Robust methods to screen and analyse membrane protein complexes are essential to shed light on the molecular mechanism of membrane protein interactions. Most methods for detecting protein:...

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Autores principales:	Florian Schmitz, Jessica Glas, Richard Neutze, Kristina Hedfalk
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1da6ce3993a549b48d559848388d9030
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spelling	oai:doaj.org-article:1da6ce3993a549b48d559848388d90302021-12-02T18:51:15ZA bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions10.1038/s41598-021-98810-22045-2322https://doaj.org/article/1da6ce3993a549b48d559848388d90302021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98810-2https://doaj.org/toc/2045-2322Abstract Interactions between membrane proteins within a cellular environment are crucial for all living cells. Robust methods to screen and analyse membrane protein complexes are essential to shed light on the molecular mechanism of membrane protein interactions. Most methods for detecting protein:protein interactions (PPIs) have been developed to target the interactions of soluble proteins. Bimolecular fluorescence complementation (BiFC) assays allow the formation of complexes involving PPI partners to be visualized in vivo, irrespective of whether or not these interactions are between soluble or membrane proteins. In this study, we report the development of a screening approach which utilizes BiFC and applies flow cytometry to characterize membrane protein interaction partners in the host Saccharomyces cerevisiae. These data allow constructive complexes to be discriminated with statistical confidence from random interactions and potentially allows an efficient screen for PPIs in vivo within a high-throughput setup.Florian SchmitzJessica GlasRichard NeutzeKristina HedfalkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Florian Schmitz Jessica Glas Richard Neutze Kristina Hedfalk A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
description	Abstract Interactions between membrane proteins within a cellular environment are crucial for all living cells. Robust methods to screen and analyse membrane protein complexes are essential to shed light on the molecular mechanism of membrane protein interactions. Most methods for detecting protein:protein interactions (PPIs) have been developed to target the interactions of soluble proteins. Bimolecular fluorescence complementation (BiFC) assays allow the formation of complexes involving PPI partners to be visualized in vivo, irrespective of whether or not these interactions are between soluble or membrane proteins. In this study, we report the development of a screening approach which utilizes BiFC and applies flow cytometry to characterize membrane protein interaction partners in the host Saccharomyces cerevisiae. These data allow constructive complexes to be discriminated with statistical confidence from random interactions and potentially allows an efficient screen for PPIs in vivo within a high-throughput setup.
format	article
author	Florian Schmitz Jessica Glas Richard Neutze Kristina Hedfalk
author_facet	Florian Schmitz Jessica Glas Richard Neutze Kristina Hedfalk
author_sort	Florian Schmitz
title	A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
title_short	A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
title_full	A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
title_fullStr	A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
title_full_unstemmed	A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
title_sort	bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1da6ce3993a549b48d559848388d9030
work_keys_str_mv	AT florianschmitz abimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT jessicaglas abimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT richardneutze abimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT kristinahedfalk abimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT florianschmitz bimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT jessicaglas bimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT richardneutze bimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions AT kristinahedfalk bimolecularfluorescencecomplementationflowcytometryscreenformembraneproteininteractions
_version_	1718377432687312896

A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions

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