Lottridge Jillian M, Flannery Andrew R, Vincelli Jennifer L, Stevens Tom H
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA.
Proc Natl Acad Sci U S A. 2006 Apr 18;103(16):6202-7. doi: 10.1073/pnas.0601712103. Epub 2006 Apr 6.
Previous two-hybrid analysis of the 17 soluble class E Vps yeast proteins revealed that Vps46p/Did2p interacts with Vta1p and the AAA (ATPase associated with a variety of cellular activities) ATPase Vps4p. Here we report that the binding of Vps46p to Vps4p and Vta1p is direct and not mediated by additional proteins, and the binding of Vps46p to Vps4p is ATP independent. Vps46p regulates the membrane association of Vps4p and is required for the interaction of Vta1p with Vps32p/Snf7p of the ESCRT-III complex. Vta1p is a potent activator of Vps4p, stimulating the ATPase activity by 6- to 8-fold. These results reveal functional roles for the Vps46p and Vta1p proteins in regulating the ESCRT complex assembly/disassembly cycle in protein sorting at the yeast late endosome.
先前对17种可溶性E类Vps酵母蛋白进行的双杂交分析表明，Vps46p/Did2p与Vta1p以及AAA（与多种细胞活动相关的ATP酶）ATP酶Vps4p相互作用。在此我们报告，Vps46p与Vps4p和Vta1p的结合是直接的，并非由其他蛋白质介导，并且Vps46p与Vps4p的结合不依赖ATP。Vps46p调节Vps4p与膜的结合，并且是Vta1p与ESCRT-III复合物的Vps32p/Snf7p相互作用所必需的。Vta1p是Vps4p的强效激活剂，可将ATP酶活性提高6至8倍。这些结果揭示了Vps46p和Vta1p蛋白在调节酵母晚期内体蛋白质分选过程中ESCRT复合物组装/拆卸循环中的功能作用。
