Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry
The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 September 2012
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| In: |
Science
Year: 2012, Jahrgang: 337, Heft: 6100, Pages: 1348-1352 |
| ISSN: | 1095-9203 |
| DOI: | 10.1126/science.1221483 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1126/science.1221483 Verlag, kostenfrei, Volltext: http://science.sciencemag.org/content/337/6100/1348 
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| Verfasserangaben: | Franz Herzog, Abdullah Kahraman, Daniel Boehringer, Raymond Mak, Andreas Bracher, Thomas Walzthoeni, Alexander Leitner, Martin Beck, Franz-Ulrich Hartl, Nenad Ban, Lars Malmström, Ruedi Aebersold |
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| 520 | |a The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adapted XL-MS protocol. Systematic analysis of human protein phosphatase 2A (PP2A) complexes identified 176 interprotein and 570 intraprotein cross-links that link specific trimeric PP2A complexes to a multitude of adaptor proteins that control their cellular functions. Spatial restraints guided molecular modeling of the binding interface between immunoglobulin binding protein 1 (IGBP1) and PP2A and revealed the topology of TCP1 ring complex (TRiC) chaperonin interacting with the PP2A regulatory subunit 2ABG. This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes. Spatial restraints revealed by chemical cross-linking and mass spectrometry elucidate the topology of a dynamic signaling network. | ||
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