One of the most fundamental features of biological systems is probably their ability to self-organize in space and time on different scales. Despite many elaborate theoretical models of how molecular self-organization can come about, only a few experimental systems of biological origin have so far been rigorously described, due mostly to their inherent complexity. The most promising strategy of modern biophysics is thus to identify minimal biological systems showing self-organized emergent behavior. One of the best-understood examples of protein self-organization, which has recently been successfully reconstituted in vitro, is represented by the oscillations of the Min proteins in Escherichia coli. In this review, we summarize the current understanding of the mechanism of Min protein self-organization in vivo and in vitro. We discuss the potential of the Min oscillations to sense the geometry of the cell and suggest that spontaneous protein waves could be a general means of intracellular organization. We hypothesize that cooperative membrane binding and unbinding, e.g., as an energy-dependent switch, may act as an important regulatory mechanism for protein oscillations and pattern formation in the cell.

中文翻译：

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蛋白质自组织：最小系统的经验教训。

生物系统最基本的特征之一可能是它们在空间和时间上以不同规模自组织的能力。尽管有许多详尽的关于分子自组织如何产生的理论模型，但由于其固有的复杂性，到目前为止，仅对少数生物学起源的实验系统进行了严格的描述。因此，现代生物物理学的最有前途的策略是识别表现出自组织突发行为的最小生物系统。最近在体外成功重构的蛋白质自组织的最容易理解的例子之一是大肠杆菌中Min蛋白的振荡。在这篇综述中，我们总结了目前对体内和体外Min蛋白自组织机制的理解。我们讨论Min振荡的潜力，以感测细胞的几何形状，并建议自发的蛋白质波可能是细胞内组织的一般手段。我们假设协作膜的结合和解除结合，例如作为能量依赖的开关，可能充当细胞中蛋白质振荡和模式形成的重要调控机制。