Regulation of a formin complex by the microtubule plus end protein tea1p.

Regulation of a formin complex by the microtubule plus end protein tea1p.
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DOI:
10.1083/jcb.200403090
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发表时间:
2004-06-07
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Chang F
Chang F
中科院分区:
其他
文献类型:
--
作者:
Feierbach B;Verde F;Chang F

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微管的正端被推测为调节肌动蛋白细胞骨架,以正确定位细胞极化和胞质分裂的位置。在裂殖酵母中,间期微管和海带重复蛋白tea1p调节极化细胞的生长。在这里,我们证明了tea1p通过微管和末端直接沉积在细胞顶端。Tea1p在大的“极化体”复合体中与bu6p和for3p结合,for3p是一种组装肌动蛋白电缆的福尔曼。Tea1p还在一个单独的复合体中与CLIP-170蛋白tip1p相互作用,Tip1p是一种微管+末端结合蛋白,将Tea1p锚定到微管+末端。定位实验表明,tea1p和bu6p调控着Forin的分布和肌动蛋白电缆的组装。虽然单个突变体仍然极化,但对于3Δbu6Δtea1Δ三个突变体的细胞无极性,表明这些蛋白质在细胞极化中贡献了重叠的功能。因此,这些实验开始阐明微管如何有助于肌动蛋白组装和极化细胞生长的适当空间调节。
The plus ends of microtubules have been speculated to regulate the actin cytoskeleton for the proper positioning of sites of cell polarization and cytokinesis. In the fission yeast Schizosaccharomyces pombe, interphase microtubules and the kelch repeat protein tea1p regulate polarized cell growth. Here, we show that tea1p is directly deposited at cell tips by microtubule plus ends. Tea1p associates in large “polarisome” complexes with bud6p and for3p, a formin that assembles actin cables. Tea1p also interacts in a separate complex with the CLIP-170 protein tip1p, a microtubule plus end–binding protein that anchors tea1p to the microtubule plus end. Localization experiments suggest that tea1p and bud6p regulate formin distribution and actin cable assembly. Although single mutants still polarize, for3Δbud6Δtea1Δ triple-mutant cells lack polarity, indicating that these proteins contribute overlapping functions in cell polarization. Thus, these experiments begin to elucidate how microtubules contribute to the proper spatial regulation of actin assembly and polarized cell growth.
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发表时间: 2002-06-28
期刊: CELL
影响因子: 64.5
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影响因子: 9.2
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期刊: CURRENT BIOLOGY
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