膜蛋白相互作用图

Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae

关于膜蛋白行为的知识对于了解真核细胞生物学及人类疾病非常重要。这篇论文显示，关于具有未知功能的膜蛋白的广泛机制信息可以通过识别它们与具有已知功能的其他蛋白的相互作用来获得。膜蛋白复合物的憎水性使它们难以用传统亲和提纯法来处理，但Andrew Emili极其同事发现，来自酿酒酵母的可溶性膜复合物能够在有三种不同非变性清洁剂存在时被亲和提纯。他们通过质谱识别出了共提纯蛋白，并且了一个有关膜蛋白相互作用的大规模物理相互作用图，其中大部分相互作用以前并未报告过。

[ 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.