A new cross-linking strategy: protein interaction reporter (PIR) technology for protein–protein interaction studies
Open accessAbstract
Chemical cross-linking coupled with mass spectrometry, an emerging approach for protein topology and interaction studies, has gained increasing interest in the past few years. A number of recent proof-of-principle studies on model proteins or protein complex systems with improved cross-linking strategies have shown great promise. However, the heterogeneity and low abundance of the cross-linked products as well as data complexity continue to pose enormous challenges for large-scale application of cross-linking approaches. A novel mass spectrometry-cleavable cross-linking strategy embodied in Protein Interaction Reporter (PIR) technology, first reported in 2005, was recently successfully applied for in vivo identification of protein–protein interactions as well as actual regions of the interacting proteins that share close proximity while present within cells. PIR technology holds great promise for achieving the ultimate goal of mapping protein interaction network at systems level using chemical cross-linking. In this review, we will briefly describe the recent progress in the field of chemical cross-linking development with an emphasis on the PIR concepts, its applications and future directions.
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Chavez et al. utilized a cross-linking strategy, Protein Interaction Reporter technology, to generate cross-links that are cleaved within a mass spectrometer for the identification of interacting protein and peptide sequences.
“Chavez et al. utilized a remarkable cross-linking strategy, Protein Interaction Reporter technology, to generate cross-links that are cleaved within a mass spectrometer for the identification of interacting protein and peptide sequences [99,100].”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [99]
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Self-citation
- Authors
- Tang, X., & Bruce, J. E.
- Affiliations
- Novo Nordisk (United States) (US)
- University of Washington (US)
- Corresponding author
- Bruce, James E
- Venue
- Molecular BioSystems
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-03-16
- Volume
- 6
- Issue
- 6
- Pages
- 939-947
- ISSN
- 1742-2051 (ISSN-L)
- 1742-206X
- PMC
- PMC3075923
- OpenAlex
- W1995233241
- Cited by
- 143
- References
- 83
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 6 · 2023: 9 · 2022: 11 · 2021: 10 · 2020: 13 · 2019: 19 · 2018: 15 · 2017: 5 · 2016: 5 · 2015: 12 · 2014: 6 · 2013: 6 · 2012: 11
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular BioSystems (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM086688)
- National Center for Research Resources (R01RR023334, S10RR025107)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Keywords
- crosslinking, protein-protein interaction, protein-protein interaction network
- MeSH terms
- Amino Acid Sequence, Binding Sites, Cross-Linking Reagents, Models, Chemical, Protein Binding, Proteins, Mass Spectrometry, Molecular Structure, Protein Interaction Mapping
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