Tsang Hilda T H, Connell James W, Brown Stephanie E, Thompson Amanda, Reid Evan, Sanderson Christopher M
Department of Medical Genetics and Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, UK.
Genomics. 2006 Sep;88(3):333-46. doi: 10.1016/j.ygeno.2006.04.003. Epub 2006 May 30.
In Saccharomyces cerevisiae 6 closely related proteins (Did2p, Vps2p, Vps24p, Vps32p, Vps60p, Vps20p) form part of the extended ESCRT III complex. This complex is required for the formation of multivesicular bodies and the degradation of internalized transmembrane receptor proteins. In contrast the human genome encodes 10 homologous proteins (CHMP1A (approved gene symbol PCOLN3), 1B, 2A, 2B, 3 (approved gene symbol VPS24), 4A, 4B, 4C, 5, and 6). In this study we have performed a series of protein interaction experiments to generate a more comprehensive picture of the human CHMP protein-interaction network. Our results describe novel interactions between known components of the human ESCRT III complex and identify a range of putative binding partners, which may indicate new ways in which the function of human CHMP proteins may be regulated. In particular, we show that two further MIT domain-containing proteins (AMSH/STAMBP and LOC129531) interact with multiple components of the human ESCRT III complex.
在酿酒酵母中,6种密切相关的蛋白质(Did2p、Vps2p、Vps24p、Vps32p、Vps60p、Vps20p)构成了扩展的内吞转运所需的分选转运蛋白复合物III(ESCRT III)的一部分。该复合物对于多囊泡体的形成以及内化跨膜受体蛋白的降解是必需的。相比之下,人类基因组编码10种同源蛋白(CHMP1A(批准的基因符号为PCOLN3)、1B、2A、2B、3(批准的基因符号为VPS24)、4A、4B、4C, 5和6)。在本研究中,我们进行了一系列蛋白质相互作用实验,以更全面地描绘人类CHMP蛋白质相互作用网络。我们的结果描述了人类ESCRT III复合物已知成分之间的新型相互作用,并鉴定出一系列假定的结合伴侣,这可能揭示了调节人类CHMP蛋白功能的新途径。特别是,我们发现另外两种含MIT结构域的蛋白质(AMSH/STAMBP和LOC129531)与人类ESCRT III复合物的多个成分相互作用。