YFR016c/Aip5 is part of an actin nucleation complex in yeast
YFR016c/Aip5 is part of an actin nucleation complex in yeast
复制标题
DOI：
10.1242/bio.044024
复制
发表时间：
2019-08-01
期刊：
影响因子：
2.4
通讯作者：
Johnsson, Nils
中科院分区：
文献类型：
--
作者：
Glomb, Oliver;Bareis, Lara;Johnsson, Nils
极性体包括在酵母和丝状真菌中组织极性生长的蛋白质网络。酵母肌动蛋白Bni 1和肌动蛋白成核促进因子Bud 6是极化体的亚基，它们一起催化酵母细胞尖端下方肌动蛋白电缆的形成。我们鉴定了YFR 016 c（Aip 5）作为Bud 6和极性体支架Spa 2的相互作用伴侣。缺乏Aip 5的酵母细胞显示出数量减少的肌动蛋白电缆。Aip 5以其N-末端区域与Spa 2结合，并以其C-末端区域与Bud 6结合。这两种相互作用合作，本地化Aip 5在芽尖和颈部，并需要刺激肌动蛋白电缆的形成。我们的实验特征Aip 5作为一个复杂的，调节肌动蛋白丝的数量在极性增长的网站的一个新的亚基。
The polarisome comprises a network of proteins that organizes polar growth in yeast and filamentous fungi. The yeast formin Bni1 and the actin nucleation-promoting factor Bud6 are subunits of the polarisome that together catalyze the formation of actin cables below the tip of yeast cells. We identified YFR016c (Aip5) as an interaction partner of Bud6 and the polarisome scaffold Spa2. Yeast cells lacking Aip5 display a reduced number of actin cables. Aip5 binds with its N-terminal region to Spa2 and with its C-terminal region to Bud6. Both interactions collaborate to localize Aip5 at bud tip and neck, and are required to stimulate the formation of actin cables. Our experiments characterize Aip5 as a novel subunit of a complex that regulates the number of actin filaments at sites of polar growth.