Differences

This shows you the differences between two versions of the page.

Link to this comparison view

Both sides previous revision Previous revision
Next revision
Previous revision
bisson2011 [2011/06/03 12:33]
biogridadmin
bisson2011 [2011/06/03 12:33]
biogridadmin
Line 1: Line 1:
 ====== A Case for the Adaptor Protein GRB2 (2011) ====== ====== A Case for the Adaptor Protein GRB2 (2011) ======
  
-Title: Quantitative Mass Spectrometry Analysis of Signalling Dynamics Using Selected Reaction Monitoring: a Case for the Adaptor Protein GRB2 - Nature Biotechnology (2011)+**Title:** Quantitative Mass Spectrometry Analysis of Signalling Dynamics Using Selected Reaction Monitoring: a Case for the Adaptor Protein GRB2 - Nature Biotechnology (2011)
  
-Authors: Nicolas Bisson, D. Andrew James, Gordana Ivosev, Stephen A. Tate, Ron Bonner, Lorne Taylor and Tony Pawson+**Authors:** Nicolas Bisson, D. Andrew James, Gordana Ivosev, Stephen A. Tate, Ron Bonner, Lorne Taylor and Tony Pawson
  
-Abstract: Signalling pathways are commonly organized through inducible protein-protein interactions,​ mediated by adaptor proteins that link activated receptors to cytoplasmic effectors. However, we have little quantitative data regarding the kinetics with which such networks assemble and dissolve to generate a specific cellular response. We have found that the GRB2 adaptor nucleates a remarkably diverse set of protein complexes, involved in multiple aspects of cellular function. To comprehensively and quantitatively investigate changes in GRB2-based protein interactions in cells, we have designed a mass spectrometry method, AP-SRM (affinity purification-selected reaction monitoring). The data define context-specific and time-dependent networks that form around GRB2 following stimulation,​ and reveal core and growth factor-selective interaction subsets. These results illustrate the reliability of AP-SRM in the quantitative analysis of dynamic signalling networks; they suggest that capturing a key hub protein and dissecting its interactions by SRM is an approach that can be broadly applied to quantify signalling dynamics. ​  +**Abstract:** Signalling pathways are commonly organized through inducible protein-protein interactions,​ mediated by adaptor proteins that link activated receptors to cytoplasmic effectors. However, we have little quantitative data regarding the kinetics with which such networks assemble and dissolve to generate a specific cellular response. We have found that the GRB2 adaptor nucleates a remarkably diverse set of protein complexes, involved in multiple aspects of cellular function. To comprehensively and quantitatively investigate changes in GRB2-based protein interactions in cells, we have designed a mass spectrometry method, AP-SRM (affinity purification-selected reaction monitoring). The data define context-specific and time-dependent networks that form around GRB2 following stimulation,​ and reveal core and growth factor-selective interaction subsets. These results illustrate the reliability of AP-SRM in the quantitative analysis of dynamic signalling networks; they suggest that capturing a key hub protein and dissecting its interactions by SRM is an approach that can be broadly applied to quantify signalling dynamics. ​  
  
 **Download (109 Interactions):​** [[http://​thebiogrid.org/​downloads/​archives/​Published%20Datasets/​Bisson2011/​Bisson_BioGRID_data_deposition.xls.zip|Microsoft Excel Format (XLS)]] **Download (109 Interactions):​** [[http://​thebiogrid.org/​downloads/​archives/​Published%20Datasets/​Bisson2011/​Bisson_BioGRID_data_deposition.xls.zip|Microsoft Excel Format (XLS)]]
  
 
bisson2011.txt · Last modified: 2017/08/08 12:52 (external edit)