Institut Curie, UMR144, 26 rue d'Ulm, 75248, Paris Cedex 05, France.
Cell Div. 2010 Sep 29;5:25. doi: 10.1186/1747-1028-5-25.
Polo-like kinase 4 (PLK4) is a unique member of the Polo-like family of kinases that shares little homology with its siblings and has an essential role in centriole duplication. The turn-over of this kinase must be strictly controlled to prevent centriole amplification. This is achieved, in part, by an autoregulatory mechanism, whereby PLK4 autophosphorylates residues in a PEST sequence located carboxy-terminal to its catalytic domain. Phosphorylated PLK4 is subsequently recognized by the SCF complex, ubiquitinylated and targeted to the proteasome for degradation. Recent data have also shown that active PLK4 is restricted to the centrosome, a mechanism that could serve to prevent aberrant centriole assembly elsewhere in the cell. While significant advances have been made in understanding how PLK4 is regulated it is certain that additional regulatory mechanisms exist to safeguard the fidelity of centriole duplication. Here, we overview past and present data discussing the regulation and functions of PLK4.
丝氨酸苏氨酸激酶 4（PLK4）是 Polo 样激酶家族的一个独特成员，与它的兄弟姐妹同源性很小，在中心体复制中起着至关重要的作用。该激酶的周转率必须受到严格控制，以防止中心体扩增。这部分是通过自动调节机制实现的，其中 PLK4 自身磷酸化位于其催化结构域羧基末端的 PEST 序列中的残基。磷酸化的 PLK4 随后被 SCF 复合物识别，泛素化并靶向蛋白酶体进行降解。最近的数据还表明，活性 PLK4 仅限于中心体，这一机制可以防止细胞内其他部位异常的中心体组装。虽然在理解 PLK4 的调节方面已经取得了重大进展，但可以肯定的是，还存在其他调节机制来保证中心体复制的保真度。在这里，我们回顾过去和现在的数据，讨论 PLK4 的调节和功能。
