Cell Polarity 1
Cell Polarity 1
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DOI：
10.1007/978-3-319-14463-4
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发表时间：
2015
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影响因子：
--
通讯作者：
K. Ebnet
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文献类型：
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作者：
K. Ebnet
上皮细胞通过机械和化学刺激感知周围环境，对多种张力和力源做出反应，包括细胞-细胞和细胞-细胞外基质（ECM）相互作用产生的张力和力源：它们通过发展顶基轴极性对这些线索做出反应。磷酸肌醇（PI）是生物膜的结构组分，其通过时空募集含有PI特异性结合结构域的效应物来控制多种信号传导途径。因此，它们已经显示出调节过多的细胞过程，包括肌动蛋白聚合、细胞迁移、增殖、分化和囊泡运输。PI在不同的膜中富集，并且它们的水平受到特定PI激酶和磷酸酶的严格调节。在过去的十年中，PI已经脱颖而出，作为特定的标志物，定义膜身份，作为细胞极化过程的关键调节剂。在这篇综述中，我们研究了PI是如何能够分配身份极化上皮细胞质膜域和整合在空间和时间复杂的信号通路，以触发适当的细胞反应的环境线索。PI涉及大量的细胞反应，这些细胞反应是形态发生的核心，例如但不限于细胞骨架变化、胞质分裂和下游效应物的募集，以控制涉及极化和管腔形成的机制。本文还讨论了病原体对极化细胞PI代谢和质膜特性的破坏以及PI研究的临床意义。
Epithelial cells sense their surrounding environment via mechanical and chemical stimuli, responding to multiple sources of tension and force, including those generated by cell–cell and cell–extracellular matrix (ECM) interaction: they respond to these cues by developing an apicobasal axis of polarity. Phosphoinositides (PIs) are structural components of biological membranes that control a diverse array of signaling pathways through spatiotemporal recruitment of effectors containing PI-specific binding domain(s). Thus they have been shown to modulate a plethora of cellular processes including actin polymerization, cell migration, proliferation, differentiation, and vesicular trafficking. PIs are enriched in different membranes and their levels are tightly regulated by specific PI kinases and phosphatases. During the past decade, PIs have come to the fore as specific markers that define membrane identity, acting as critical regulators of the cell polarization process. In this review, we have examined how PIs are able to assign identity to polarized epithelial cell plasma membrane domains and integrate in space and time complex signaling pathways to trigger appropriate cellular responses to environmental cues. PIs are implicated in a vast array of cellular responses that are central for morphogenesis such as, but not limited to, cytoskeletal changes, cytokinesis, and recruitment of downstream effectors to govern mechanisms involved in polarization and lumen formation. Subversion by pathogens of PI metabolism and plasma membrane identity in polarized cells and the clinical relevance of research on PIs were also discussed.