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                	 Deciphering Preferential 
                		Interactions within Supramolecular Protein Complexes: the Proteasome Case 
                  Bertrand Fabre, Thomas Lambour, Luc Garrigues, François Amalric, Nathalie Vigneron, 
                  	Thomas Menneteau, Alexandre Stella, Bernard Monsarrat, Benoît Van den Eynde, Odile Burlet-Schiltz, 
                  	& Marie-Pierre Bousquet-Dubouch 
                  Molecular Systems Biology (2015) 11: 771 
                  Proteasomes are dynamic structures and adapt to their diverse biological contexts by 
                  	changing their overall subunit composition and association with regulatory particles and interacting proteins. 
                  	This high level of proteasome diversity could reflect specialized functions of each individual proteasome form. 
                  This paper demonstrates an approach to decipher proteasome heterogeneity through label-free 
                  	quantitative proteomics.  The authors analyzed sub-complex composition by combining affinity purification and 
                  	protein abundance correlation profiling with high-resolution mass spectrometry.  By correlating proteins 
                  	abundances across a large set of 24 proteasome samples immunopurified from nine different human cell lines, 
                  	they observed that the two main 20S proteasome subtypes, sP20S and iP20S, interact with a different 
                  	subset of regulators. This approach could be applied to other important large complexes. 
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