Dept. of Human Molecular Genetics and Biochemistry, Tel Aviv University, Tel Aviv 69978, Israel.
Curr Opin Cell Biol. 2012 Oct;24(5):562-8. doi: 10.1016/j.ceb.2012.05.004. Epub 2012 Jun 22.
Cell biologists studying cell adhesion have already figured out that cell-extracellular matrix connections, mediated by integrin receptors, are diverse and extremely complex structures. Dozens of adaptors-linking integrins with the cytoskeleton, and numerous enzymes and signaling proteins-regulating adhesion site dynamics, collectively referred to as the integrin adhesome, cooperate in mediating adhesion and activating specific signaling networks. Recent proteomic studies indicate that the known adhesome complexity is just the tip of the iceberg. In each existing category of molecular function the number of candidate components more than double the known components and several new categories are suggested. Proteomic analysis of different integrin heterodimers points to integrin-specific variations in composition and analysis of adhesion complexes under varying tension regimes highlights the force-dependent recruitment of different components, most notably LIM domain proteins.
研究细胞黏附的细胞生物学家已经发现，整合素受体介导的细胞-细胞外基质连接是多种多样且极其复杂的结构。数十种衔接蛋白将整合素与细胞骨架连接起来，还有许多调节黏附部位动态的酶和信号蛋白——统称为整合素黏着斑，共同介导黏附并激活特定的信号网络。最近的蛋白质组学研究表明，已知的黏着斑的复杂性只是冰山一角。在每个现有的分子功能类别中，候选成分的数量都比已知成分多一倍以上，并且还提出了几个新的类别。不同整合素异二聚体的蛋白质组学分析表明，组成存在整合素特异性变化，在不同张力状态下分析黏附复合物则突出了不同成分的力依赖性募集，尤其是 LIM 结构域蛋白。
