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September 25, 2014Molecular & Cellular ProteomicsOpen Access

A New in Vivo Cross-linking Mass Spectrometry Platform to Define Protein–Protein Interactions in Living Cells

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Authors

RKRobyn M. KaakeXWXiaorong WangABAnthony M. Burke

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Overview

Experimental study reveals a cross-linking mass spectrometry platform for capturing protein interactions in living mammalian cells, highlighting a pathway toward mapping cellular interactomes.

Key Points

  • To establish an in vivo cross-linking mass spectrometry platform capable of capturing and identifying protein–protein interactions and interaction interfaces directly within living mammalian cells.
  • Synthesized and implemented a membrane-permeable, enrichable, and mass spectrometry-cleavable chemical cross-linker.
  • Coupled cross-linker enrichment with multistage tandem mass spectrometry to capture, isolate, and sequence cross-linked protein products from mammalian cells across targeted complexes and proteome-wide scales.
  • Enabled the direct capture, enrichment, and identification of in vivo cross-linked products from intact mammalian cells.
  • Successfully determined physical protein interaction interfaces at both targeted multi-protein complex levels and across the broader proteome.

Cite This Study

Kaake et al. (2014) studied this question.

synapsesocial.com/papers/69fe4a2cc4de4e0170011743https://doi.org/10.1074/mcp.m114.042630
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