University of Geneva, Department of Cell Physiology and Metabolism, Centre Médical Universitaire, 1. Rue Michel-Servet, 1211 Geneva 4, Switzerland.
Curr Opin Cell Biol. 2012 Feb;24(1):116-24. doi: 10.1016/j.ceb.2011.11.001. Epub 2011 Dec 2.
Integrin-dependent cell adhesions come in different shapes and serve in different cell types for tasks ranging from cell-adhesion, migration, and the remodeling of the extracellular matrix to the formation and stabilization of immunological and chemical synapses. A major challenge consists in the identification of adhesion-specific as well as common regulatory mechanisms, motivating the need for a deeper analysis of protein-protein interactions in the context of intact focal adhesions. Specifically, it is critical to understand how small differences in binding of integrins to extracellular ligands and/or cytoplasmic adapter proteins affect the assembly and function of an entire focal adhesion. By using the talin-integrin pair as a starting point, I would like to discuss how specific protein-protein and protein-lipid interactions can control the behavior and function of focal adhesions. By responding to chemical and mechanical cues several allosterically regulated proteins create a dynamic multifunctional protein network that provides both adhesion to the extracellular matrix as well as intracellular signaling in response to mechanical changes in the cellular environment.
整合素依赖的细胞黏附具有不同的形态，在不同的细胞类型中发挥作用，包括细胞黏附、迁移和细胞外基质重塑，以及免疫和化学突触的形成和稳定。一个主要的挑战在于确定黏附特异性和共同的调节机制，这促使我们需要更深入地分析完整黏着斑中蛋白质-蛋白质相互作用。具体来说，理解整合素与细胞外配体和/或细胞质衔接蛋白的结合微小差异如何影响整个黏着斑的组装和功能是至关重要的。我想以 talin-integrin 对作为起点，讨论特定的蛋白质-蛋白质和蛋白质-脂质相互作用如何控制黏着斑的行为和功能。通过对化学和机械线索的反应，几个变构调节的蛋白质形成了一个动态的多功能蛋白质网络，为细胞外基质的黏附和对细胞环境中机械变化的细胞内信号提供了响应。
