Abstract
Background: mTORC1 recruits its substrate 4E-BP1 via Raptor/4E-BP1 interaction. Chemical cross-linking/mass spectrometry permits characterization of protein-protein interactions. Results: Cross-linked peptides between Raptor and 4E-BP1 were identified. Raptor intramolecular cross-links were also identified. Conclusion: Raptor N-terminal region containing RNC1 is implicated in the interaction with the central region of 4E-BP1. Significance: Our study provides novel insight into how mTORC1 recognizes 4E-BP1. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Coffman, K., Yang, B., Lu, J., Tetlow, A. L., Pelliccio, E., Lu, S., … Tamanoi, F. (2014). Characterization of the raptor/4E-BP1 interaction by chemical cross-linking coupled with mass spectrometry analysis. Journal of Biological Chemistry, 289(8), 4723–4734. https://doi.org/10.1074/jbc.M113.482067
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