Khan Rejina B, Goult Benjamin T
School of Biosciences, University of Kent, Canterbury, United Kingdom.
Front Mol Biosci. 2019 Dec 17;6:144. doi: 10.3389/fmolb.2019.00144. eCollection 2019.
The advent of cell-cell and cell-extracellular adhesion enabled cells to interact in a coherent manner, forming larger structures and giving rise to the development of tissues, organs and complex multicellular life forms. The development of such organisms required tight regulation of dynamic adhesive structures by signaling pathways that coordinate cell attachment. Integrin-mediated adhesion to the extracellular matrix provides cells with support, survival signals and context-dependent cues that enable cells to run different cellular programs. One mysterious aspect of the process is how hundreds of proteins assemble seemingly spontaneously onto the activated integrin. An emerging concept is that adhesion assembly is regulated by autoinhibition of key proteins, a highly dynamic event that is modulated by a variety of signaling events. By enabling precise control of the activation state of proteins, autoinhibition enables localization of inactive proteins and the formation of pre-complexes. In response to the correct signals, these proteins become active and interact with other proteins, ultimately leading to development of cell-matrix junctions. Autoinhibition of key components of such adhesion complexes-including core components integrin, talin, vinculin, and FAK and important peripheral regulators such as RIAM, Src, and DLC1-leads to a view that the majority of proteins involved in complex assembly might be regulated by intramolecular interactions. Autoinhibition is relieved via multiple different signals including post-translation modification and proteolysis. More recently, mechanical forces have been shown to stabilize and increase the lifetimes of active conformations, identifying autoinhibition as a means of encoding mechanosensitivity. The complexity and scope for nuanced adhesion dynamics facilitated via autoinhibition provides numerous points of regulation. In this review, we discuss what is known about this mode of regulation and how it leads to rapid and tightly controlled assembly and disassembly of cell-matrix adhesion.
细胞间和细胞与细胞外基质的黏附的出现,使细胞能够以协调一致的方式相互作用,形成更大的结构,并促使组织、器官和复杂的多细胞生命形式的发育。这类生物体的发育需要通过协调细胞附着的信号通路对动态黏附结构进行严格调控。整合素介导的与细胞外基质的黏附为细胞提供支持、生存信号和依赖于环境的线索,使细胞能够运行不同的细胞程序。这个过程的一个神秘之处在于,数百种蛋白质如何看似自发地组装到活化的整合素上。一个新兴的概念是,黏附组装受关键蛋白质的自抑制调节,这是一个高度动态的事件,受多种信号事件的调节。通过精确控制蛋白质的激活状态,自抑制使无活性蛋白质得以定位并形成预复合物。响应正确的信号,这些蛋白质变得活跃并与其他蛋白质相互作用,最终导致细胞-基质连接的形成。对这类黏附复合物的关键成分(包括核心成分整合素、踝蛋白、纽蛋白和黏着斑激酶以及重要的外周调节因子如RIAM、Src和DLC1)的自抑制导致这样一种观点,即参与复合物组装的大多数蛋白质可能受分子内相互作用的调节。自抑制通过多种不同信号得以解除,包括翻译后修饰和蛋白水解。最近,机械力已被证明能稳定并延长活性构象的寿命,这表明自抑制是一种编码机械敏感性的方式。通过自抑制促进的黏附动力学的复杂性和细微差别提供了众多调控点。在本综述中,我们讨论了关于这种调节模式的已知信息,以及它如何导致细胞-基质黏附的快速且严格受控的组装和解离。