A New In Vivo Cross-linking Mass Spectrometry Platform to Define Protein-Protein Interactions in Living Cells. Kaake, R. M., Wang, X., Burke, A., Yu, C., Kandur, W., Yang, Y., Novtisky, E. J., Second, T., Duan, J., Kao, A., Guan, S., Vellucci, D., Rychnovsky, S. D., & Huang, L. Molecular & Cellular Proteomics, January, 2014. ![A New In Vivo Cross-linking Mass Spectrometry Platform to Define Protein-Protein Interactions in Living Cells [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Protein-protein interactions (PPIs) are fundamental to the structure and function of protein complexes. Resolving the physical contacts between proteins as they occur in cells is critical to uncovering the molecular details underlying various cellular activities. To advance the study of PPIs in living cells, we have developed a new in vivo cross-linking mass spectrometry platform that couples a novel membrane permeable, enrichable and MS-cleavable cross-linker with multistage tandem mass spectrometry. This strategy permits the effective capture, enrichment, and identification of in vivo cross-linked products from mammalian cells, and thus enables the determination of protein interaction interfaces. The utility of the developed method has been demonstrated by profiling PPIs in mammalian cells at the proteome scale and the targeted protein complex level. Our work represents a general approach in studying in vivo PPIs, and provides a solid foundation for future studies towards the complete mapping of PPI networks in living systems.
@article{kaake_new_2014,
title = {A {New} {In} {Vivo} {Cross}-linking {Mass} {Spectrometry} {Platform} to {Define} {Protein}-{Protein} {Interactions} in {Living} {Cells}},
copyright = {Copyright © 2014, The American Society for Biochemistry and Molecular Biology},
issn = {1535-9476, 1535-9484},
url = {http://www.mcponline.org/content/early/2014/09/24/mcp.M114.042630},
doi = {10.1074/mcp.M114.042630},
abstract = {Protein-protein interactions (PPIs) are fundamental to the structure and function of protein complexes. Resolving the physical contacts between proteins as they occur in cells is critical to uncovering the molecular details underlying various cellular activities. To advance the study of PPIs in living cells, we have developed a new in vivo cross-linking mass spectrometry platform that couples a novel membrane permeable, enrichable and MS-cleavable cross-linker with multistage tandem mass spectrometry. This strategy permits the effective capture, enrichment, and identification of in vivo cross-linked products from mammalian cells, and thus enables the determination of protein interaction interfaces. The utility of the developed method has been demonstrated by profiling PPIs in mammalian cells at the proteome scale and the targeted protein complex level. Our work represents a general approach in studying in vivo PPIs, and provides a solid foundation for future studies towards the complete mapping of PPI networks in living systems.},
language = {en},
urldate = {2019-01-07TZ},
journal = {Molecular \& Cellular Proteomics},
author = {Kaake, Robyn M. and Wang, Xiaorong and Burke, Anthony and Yu, Clinton and Kandur, Wynne and Yang, Yingying and Novtisky, Eric J. and Second, Tonya and Duan, Jicheng and Kao, Athit and Guan, Shenheng and Vellucci, Danielle and Rychnovsky, Scott D. and Huang, Lan},
month = jan,
year = {2014},
pmid = {25253489},
keywords = {Chemical biology, Crosslinking, Mass Spectrometry, Protein Cross-linking*, Protein Machines*, Protein-Protein Interactions*},
pages = {mcp.M114.042630}
}
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To advance the study of PPIs in living cells, we have developed a new in vivo cross-linking mass spectrometry platform that couples a novel membrane permeable, enrichable and MS-cleavable cross-linker with multistage tandem mass spectrometry. This strategy permits the effective capture, enrichment, and identification of in vivo cross-linked products from mammalian cells, and thus enables the determination of protein interaction interfaces. The utility of the developed method has been demonstrated by profiling PPIs in mammalian cells at the proteome scale and the targeted protein complex level. 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