Details

Autor(en) / Beteiligte

• Babu, Mohan
• Vlasblom, James
• Pu, Shuye
• Guo, Xinghua
• Graham, Chris
• Bean, Björn D. M.
• Burston, Helen E.
• Vizeacoumar, Franco J.
• Snider, Jamie
• Phanse, Sadhna
• Fong, Vincent
• Tam, Yuen Yi C.
• Davey, Michael
• Hnatshak, Olha
• Bajaj, Navgeet
• Chandran, Shamanta
• Punna, Thanuja
• Christopolous, Constantine
• Wong, Victoria
• Yu, Analyn
• Zhong, Gouqing
• Li, Joyce
• Stagljar, Igor
• Conibear, Elizabeth
• Wodak, Shoshana J.
• Emili, Andrew
• Greenblatt, Jack F.

Titel

Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae

Ist Teil von

• Nature (London), 2012-09, Vol.489 (7417), p.585-589

Ort / Verlag

London: Nature Publishing Group UK

Erscheinungsjahr

2012

Quelle

EBSCOhost Psychology and Behavioral Sciences Collection

Beschreibungen/Notizen

• A survey of 1,590 putative integral, peripheral and lipid-anchored membrane proteins from Saccharomyces cerevisiae reveals unexpected physical associations underlying the membrane biology of eukaryotes and delineates the global topological landscape of the membrane interactome. Mapping membrane protein interactions Affinity purification procedures have been successfully used to characterize soluble protein complexes, but complexes involving membrane proteins are more difficult to purify due to their hydrophobic nature. Here, Andrew Emili and colleagues have affinity purified membrane proteins from the yeast Saccharomyces cerevisiae in the presence of three different non-denaturing detergents, and identified the co-purifying proteins by mass spectrometry. They generate an extensive physical interaction map of membrane protein interactions, most of which have not been previously reported. Macromolecular assemblies involving membrane proteins (MPs) serve vital biological roles and are prime drug targets in a variety of diseases 1 . 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.