A general method to quantify ligand-driven oligomerization from fluorescence-based images
Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and t...
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| Published in | Nature methods Vol. 16; no. 6; pp. 493 - 496 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
New York
Nature Publishing Group US
01.06.2019
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein–protein interactions.
Fluorescence intensity fluctuation spectrometry provides a rapid and accurate measurement of the identity, abundance and stability of protein oligomers. |
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| AbstractList | Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein-protein interactions. Fluorescence intensity fluctuation spectrometry provides a rapid and accurate measurement of the identity, abundance and stability of protein oligomers. Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein-protein interactions. Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein–protein interactions. Fluorescence intensity fluctuation spectrometry provides a rapid and accurate measurement of the identity, abundance and stability of protein oligomers. Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein-protein interactions.Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein-protein interactions. Here we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance, and stability of protein oligomers. This approach was tested on monomers and oligomers of known sizes and was used to uncover the oligomeric states of the epidermal growth factor receptor and the secretin receptor in the presence and absence of their agonist ligands. This method is fast and is scalable for high-throughput screening of drugs targeting protein-protein interactions. |
| Audience | Academic |
| Author | Eis, Annie Popa, Ionel Biener, Gabriel Ward, Richard J. Badu, Dammar Stoneman, Michael R. Milligan, Graeme Raicu, Valerică Pediani, John D. |
| AuthorAffiliation | 2 Centre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, Scotland, UK 3 Department of Biological Sciences, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA 1 Physics Department, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA |
| AuthorAffiliation_xml | – name: 2 Centre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, Scotland, UK – name: 3 Department of Biological Sciences, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA – name: 1 Physics Department, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA |
| Author_xml | – sequence: 1 givenname: Michael R. surname: Stoneman fullname: Stoneman, Michael R. organization: Physics Department, University of Wisconsin-Milwaukee – sequence: 2 givenname: Gabriel surname: Biener fullname: Biener, Gabriel organization: Physics Department, University of Wisconsin-Milwaukee – sequence: 3 givenname: Richard J. surname: Ward fullname: Ward, Richard J. organization: Centre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow – sequence: 4 givenname: John D. orcidid: 0000-0001-6615-537X surname: Pediani fullname: Pediani, John D. organization: Centre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow – sequence: 5 givenname: Dammar surname: Badu fullname: Badu, Dammar organization: Physics Department, University of Wisconsin-Milwaukee – sequence: 6 givenname: Annie surname: Eis fullname: Eis, Annie organization: Physics Department, University of Wisconsin-Milwaukee – sequence: 7 givenname: Ionel orcidid: 0000-0003-3111-4716 surname: Popa fullname: Popa, Ionel organization: Physics Department, University of Wisconsin-Milwaukee – sequence: 8 givenname: Graeme orcidid: 0000-0002-6946-3519 surname: Milligan fullname: Milligan, Graeme organization: Centre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow – sequence: 9 givenname: Valerică orcidid: 0000-0002-3427-8516 surname: Raicu fullname: Raicu, Valerică email: vraicu@uwm.edu organization: Physics Department, University of Wisconsin-Milwaukee, Department of Biological Sciences, University of Wisconsin-Milwaukee |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31110281$$D View this record in MEDLINE/PubMed |
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| Copyright | The Author(s), under exclusive licence to Springer Nature America, Inc. 2019 COPYRIGHT 2019 Nature Publishing Group The Author(s), under exclusive licence to Springer Nature America, Inc. 2019. |
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| Snippet | Here, we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance and stability of protein oligomers. This approach... Here we introduce fluorescence intensity fluctuation spectrometry for determining the identity, abundance, and stability of protein oligomers. This approach... |
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| SubjectTerms | 631/1647/328/1978 631/1647/328/2057 631/1647/527/1819 Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology Brief Communication Drug delivery Drug screening Epidermal growth factor ErbB Receptors - chemistry ErbB Receptors - metabolism Fluorescence Growth factors High-throughput screening Humans Image Processing, Computer-Assisted - methods Life Sciences Ligands Membrane proteins Methods Microscopy, Confocal Monomers Oligomerization Oligomers Protein Binding Protein interaction Protein Interaction Domains and Motifs Protein Multimerization Protein-protein interactions Proteins Proteomics Receptors, G-Protein-Coupled - metabolism Receptors, Gastrointestinal Hormone - metabolism Secretin Signal Transduction Spectrometry Spectrometry, Fluorescence Variation |
| Title | A general method to quantify ligand-driven oligomerization from fluorescence-based images |
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