Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae - PubMed
- ️Sun Jan 01 2012
. 2012 Sep 27;489(7417):585-9.
doi: 10.1038/nature11354. Epub 2012 Sep 2.
James Vlasblom, Shuye Pu, Xinghua Guo, Chris Graham, Björn D M Bean, Helen E Burston, Franco J Vizeacoumar, Jamie Snider, Sadhna Phanse, Vincent Fong, Yuen Yi C Tam, Michael Davey, Olha Hnatshak, Navgeet Bajaj, Shamanta Chandran, Thanuja Punna, Constantine Christopolous, Victoria Wong, Analyn Yu, Gouqing Zhong, Joyce Li, Igor Stagljar, Elizabeth Conibear, Shoshana J Wodak, Andrew Emili, Jack F Greenblatt
Affiliations
- PMID: 22940862
- DOI: 10.1038/nature11354
Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae
Mohan Babu et al. Nature. 2012.
Abstract
Macromolecular assemblies involving membrane proteins (MPs) serve vital biological roles and are prime drug targets in a variety of diseases. Large-scale affinity purification studies of soluble-protein complexes have been accomplished for diverse model organisms, but no global characterization of MP-complex membership has been described so far. Here we report a complete survey of 1,590 putative integral, peripheral and lipid-anchored MPs from Saccharomyces cerevisiae, which were affinity purified in the presence of non-denaturing detergents. The identities of the co-purifying proteins were determined by tandem mass spectrometry and subsequently used to derive a high-confidence physical interaction map encompassing 1,726 membrane protein-protein interactions and 501 putative heteromeric complexes associated with the various cellular membrane systems. Our analysis reveals unexpected physical associations underlying the membrane biology of eukaryotes and delineates the global topological landscape of the membrane interactome.
Comment in
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Interactomes by mass spectrometry.
Doerr A. Doerr A. Nat Methods. 2012 Nov;9(11):1043. doi: 10.1038/nmeth.2235. Nat Methods. 2012. PMID: 23281565 No abstract available.
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