關于膜蛋白行為的知識對于了解真核細胞生物學及人類疾病非常重要。這篇論文顯示，關于具有未知功能的膜蛋白的廣泛機制信息可以通過識別它們與具有已知功能的其他蛋白的相互作用來獲得。膜蛋白復合物的憎水性使它們難以用傳統親和提純法來處理，但Andrew Emili極其同事發現，來自釀酒酵母的可溶性膜復合物能夠在有三種不同非變性清潔劑存在時被親和提純。他們通過質譜識別出了共提純蛋白，并且了一個有關膜蛋白相互作用的大規模物理相互作用圖，其中大部分相互作用以前并未報告過。
[ Macromolecular assemblies involving membrane proteins （MPs） serve vital biological roles and are prime drug targets in a variety of diseases1. 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.
