aPKC: the Kinase that Phosphorylates Cell Polarity.
aPKC: the Kinase that Phosphorylates Cell Polarity.
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DOI：
10.12688/f1000research.14427.1
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发表时间：
2018-01-01
期刊：
影响因子：
--
通讯作者：
Hong, Yang
中科院分区：
文献类型：
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作者：
Hong, Yang
建立和维持细胞极性是一个动态过程，需要复杂但高度调控的蛋白质相互作用。磷酸化是细胞控制靶蛋白功能和亚细胞定位的重要机制，多种激酶在细胞极性中起着关键作用。其中，非典型蛋白激酶C（aPKC）可能是细胞极性中研究最多的激酶，并且迄今为止具有最多的下游底物。超过一半的极性蛋白是必不可少的调节细胞极性已被确定为aPKC底物。本文主要综述了aPKC在蠕虫单细胞胚胎中调节前后极性、在上皮细胞和不对称分裂细胞（如果蝇神经母细胞）中调节顶基极性的研究。我们将通过细胞极性中的aPKC靶蛋白，并讨论aPKC磷酸化控制其亚细胞定位和生物学功能的各种机制。我们还将回顾最近的进展，确定详细的分子机制，在空间和时间控制的aPKC亚细胞定位和激酶活性在细胞极化。
Establishing and maintaining cell polarity are dynamic processes that necessitate complicated but highly regulated protein interactions. Phosphorylation is a powerful mechanism for cells to control the function and subcellular localization of a target protein, and multiple kinases have played critical roles in cell polarity. Among them, atypical protein kinase C (aPKC) is likely the most studied kinase in cell polarity and has the largest number of downstream substrates characterized so far. More than half of the polarity proteins that are essential for regulating cell polarity have been identified as aPKC substrates. This review covers mainly studies of aPKC in regulating anterior-posterior polarity in the worm one-cell embryo and apical-basal polarity in epithelial cells and asymmetrically dividing cells (for example, Drosophila neuroblasts). We will go through aPKC target proteins in cell polarity and discuss various mechanisms by which aPKC phosphorylation controls their subcellular localizations and biological functions. We will also review the recent progress in determining the detailed molecular mechanisms in spatial and temporal control of aPKC subcellular localization and kinase activity during cell polarization.