Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics
Protein-protein interactions are at the core of all cellular functions and dynamic alterations in protein interactions regulate cellular signaling. In the last decade, mass spectrometry-based proteomics has delivered unprecedented insights into human protein interaction networks. Affinity purificati...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-12-01
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| Series: | Frontiers in Genetics |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fgene.2015.00344/full |
| _version_ | 1819267947470782464 |
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| author | Jiwen eYang Sebastian Alexander Wagner Petra eBeli |
| author_facet | Jiwen eYang Sebastian Alexander Wagner Petra eBeli |
| author_sort | Jiwen eYang |
| collection | DOAJ |
| description | Protein-protein interactions are at the core of all cellular functions and dynamic alterations in protein interactions regulate cellular signaling. In the last decade, mass spectrometry-based proteomics has delivered unprecedented insights into human protein interaction networks. Affinity purification-mass spectrometry has been extensively employed for focused and high-throughput studies of steady state protein-protein interactions. Future challenges remain in mapping transient protein interactions after cellular perturbations as well as in resolving the spatial organization of protein interaction networks. Affinity purification-mass spectrometry can be combined with quantitative proteomics approaches to determine the relative abundance of purified proteins in different conditions, thereby enabling the identification of transient protein interactions. In addition to affinity purification, methods based on protein co-fractionation have been combined with quantitative mass spectrometry to map transient protein interactions during cellular signaling. More recently, approaches based on proximity tagging that preserve the spatial dimension of protein interaction networks have been introduced. Here, we provide an overview of mass spectrometry-based methods for analyzing protein-protein interactions with a focus on approaches that aim to dissect the temporal and spatial aspects of protein interaction networks. |
| first_indexed | 2024-12-23T21:25:16Z |
| format | Article |
| id | doaj.art-d14c4e525ae647c788e847185e8aec93 |
| institution | Directory Open Access Journal |
| issn | 1664-8021 |
| language | English |
| last_indexed | 2024-12-23T21:25:16Z |
| publishDate | 2015-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Genetics |
| spelling | doaj.art-d14c4e525ae647c788e847185e8aec932022-12-21T17:30:38ZengFrontiers Media S.A.Frontiers in Genetics1664-80212015-12-01610.3389/fgene.2015.00344165118Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomicsJiwen eYang0Sebastian Alexander Wagner1Petra eBeli2Institute of Molecular Biology (IMB)Goethe UniversityInstitute of Molecular Biology (IMB)Protein-protein interactions are at the core of all cellular functions and dynamic alterations in protein interactions regulate cellular signaling. In the last decade, mass spectrometry-based proteomics has delivered unprecedented insights into human protein interaction networks. Affinity purification-mass spectrometry has been extensively employed for focused and high-throughput studies of steady state protein-protein interactions. Future challenges remain in mapping transient protein interactions after cellular perturbations as well as in resolving the spatial organization of protein interaction networks. Affinity purification-mass spectrometry can be combined with quantitative proteomics approaches to determine the relative abundance of purified proteins in different conditions, thereby enabling the identification of transient protein interactions. In addition to affinity purification, methods based on protein co-fractionation have been combined with quantitative mass spectrometry to map transient protein interactions during cellular signaling. More recently, approaches based on proximity tagging that preserve the spatial dimension of protein interaction networks have been introduced. Here, we provide an overview of mass spectrometry-based methods for analyzing protein-protein interactions with a focus on approaches that aim to dissect the temporal and spatial aspects of protein interaction networks.http://journal.frontiersin.org/Journal/10.3389/fgene.2015.00344/fullprotein-protein interactionsspatial interactionsquantitative mass spectrometrymass spectrometry-based proteomicsTransient interactions |
| spellingShingle | Jiwen eYang Sebastian Alexander Wagner Petra eBeli Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics Frontiers in Genetics protein-protein interactions spatial interactions quantitative mass spectrometry mass spectrometry-based proteomics Transient interactions |
| title | Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics |
| title_full | Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics |
| title_fullStr | Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics |
| title_full_unstemmed | Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics |
| title_short | Illuminating spatial and temporal organization of protein interaction networks by mass spectrometry-based proteomics |
| title_sort | illuminating spatial and temporal organization of protein interaction networks by mass spectrometry based proteomics |
| topic | protein-protein interactions spatial interactions quantitative mass spectrometry mass spectrometry-based proteomics Transient interactions |
| url | http://journal.frontiersin.org/Journal/10.3389/fgene.2015.00344/full |
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