The actin cytoskeleton is a target of the self-incompatibility response in Papaver rhoeas.
The actin cytoskeleton is a target of the self-incompatibility response in Papaver rhoeas.
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DOI：
10.1093/jxb/erg003
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发表时间：
2003
影响因子：
6.9
通讯作者：
C. Staiger;V. Franklin-Tong
中科院分区：
文献类型：
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作者：
C. Staiger;V. Franklin-Tong
细胞接收到的信号的整合及其转导对所有细胞反应都是必不可少的。细胞骨架已被确定为动物和植物细胞信号级联反应的主要靶点。罂粟的自交不亲和性涉及柱头s蛋白与花粉之间的等位基因特异性识别，从而抑制不亲和性花粉。当柱头s蛋白与不相容花粉相互作用时，这种高度特异性的反应会触发Ca（2+）依赖性信号级联反应。最近已经证明，SI诱导花粉肌动蛋白细胞骨架的组织发生了戏剧性的变化。这暗示肌动蛋白细胞骨架是si刺激信号的关键靶点。此处描述了肌动蛋白细胞骨架的细胞学改变，这是对SI的反应，似乎有几个阶段是可区分的。得到的证据表明，f -肌动蛋白解聚也被刺激。目前的理解，肌动蛋白细胞骨架是一个目标的信号触发的SI反应进行了讨论。这表明这些f -肌动蛋白的改变可能是Ca（2+）介导的，这可能是si诱导的尖端生长抑制实现的机制。讨论了肌动蛋白结合蛋白作为这种反应的关键介质的潜力，并描述了可能负责影响这些变化的机制。特别是，在SI和动物细胞凋亡过程中持续的肌动蛋白重排之间的相似之处被考虑。
The integration of signals received by a cell, and their transduction to targets, is essential for all cellular responses. The cytoskeleton has been identified as a major target of signalling cascades in both animal and plant cells. Self-incompatibility (SI) in Papaver rhoeas involves an allele-specific recognition between stigmatic S-proteins and pollen, resulting in the inhibition of incompatible pollen. This highly specific response triggers a Ca(2+)-dependent signalling cascade in incompatible pollen when a stigmatic S-protein interacts with it. It has been demonstrated recently that SI induces dramatic alterations in the organization of the pollen actin cytoskeleton. This implicates the actin cytoskeleton as a key target for the SI-stimulated signals. The cytological alterations to the actin cytoskeleton that are triggered in response to SI are described here and there seem to be several stages that are distinguishable temporally. Evidence was obtained that F-actin depolymerization is also stimulated. The current understanding that the actin cytoskeleton is a target for the signals triggered by the SI response is discussed. It is suggested that these F-actin alterations may be Ca(2+)-mediated and that this could be a mechanism whereby SI-induced tip growth inhibition is achieved. The potential for actin-binding proteins to act as key mediators of this response is discussed and the mechanisms that may be responsible for effecting these changes are described. In particular, the parallels between sustained actin rearrangements during SI and in apoptosis of animal cells are considered.