Systematic Characterization of the Protein Interaction Network and Protein Complexes in Saccharomyces cerevisiae Using Tandem Affinity Purification and Mass Spectrometry

Author(s):  
Mohan Babu ◽  
Nevan J. Krogan ◽  
Donald E. Awrey ◽  
Andrew Emili ◽  
Jack F. Greenblatt
2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Dorothy M. Tappenden ◽  
Hye Jin Hwang ◽  
Longlong Yang ◽  
Russell S. Thomas ◽  
John J. LaPres

The aryl-hydrocarbon receptor (AHR), a ligand activated PAS superfamily transcription factor, mediates most, if not all, of the toxicity induced upon exposure to various dioxins, dibenzofurans, and planar polyhalogenated biphenyls. While AHR-mediated gene regulation plays a central role in the toxic response to dioxin exposure, a comprehensive understanding of AHR biology remains elusive. AHR-mediated signaling starts in the cytoplasm, where the receptor can be found in a complex with the heat shock protein of 90 kDa (Hsp90) and the immunophilin-like protein, aryl-hydrocarbon receptor-interacting protein (AIP). The role these chaperones and other putative interactors of the AHR play in the toxic response is not known. To more comprehensively define the AHR-protein interaction network (AHR-PIN) and identify other potential pathways involved in the toxic response, a proteomic approach was undertaken. Using tandem affinity purification (TAP) and mass spectrometry we have identified several novel protein interactions with the AHR. These interactions physically link the AHR to proteins involved in the immune and cellular stress responses, gene regulation not mediated directly via the traditional AHR:ARNT heterodimer, and mitochondrial function. This new insight into the AHR signaling network identifies possible secondary signaling pathways involved in xenobiotic-induced toxicity.


2002 ◽  
Vol 1 (3) ◽  
pp. 204-212 ◽  
Author(s):  
Anna Shevchenko ◽  
Daniel Schaft ◽  
Assen Roguev ◽  
W. W. M. Pim Pijnappel ◽  
A. Francis Stewart ◽  
...  

2020 ◽  
Author(s):  
Harper not provided not provided JW

Analysis of protein complexes by mass spectrometry provides a powerful approach for identifying proteins that associate with other proteins. Frequently, this can be done by expressing the protein of interest with an epitope tag, such as a Hemagglutinin-A (HA) epitope, using either a stably expressed lentivirus or by gene editing the HA epitope into the gene of interest. The protocol has been used extensively to create the Bioplex protein interaction network [Huttlin et al Nature. 545:505-509 (2017); Huttlin et al Cell, 162: 425-440 (2015)].


2019 ◽  
Vol 96 (1) ◽  
Author(s):  
Guillaume Adelmant ◽  
Brijesh K. Garg ◽  
Maria Tavares ◽  
Joseph D. Card ◽  
Jarrod A. Marto

Structure ◽  
2015 ◽  
Vol 23 (4) ◽  
pp. 762-773 ◽  
Author(s):  
Arti T. Navare ◽  
Juan D. Chavez ◽  
Chunxiang Zheng ◽  
Chad R. Weisbrod ◽  
Jimmy K. Eng ◽  
...  

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