Department of Molecular Medicine, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.
EMBO Rep. 2011 Mar;12(3):259-66. doi: 10.1038/embor.2011.5. Epub 2011 Feb 11.
A characteristic of integrins is their ability to transfer chemical and mechanical signals across the plasma membrane. Force generated by myosin II makes cells able to sense substrate stiffness and induce maturation of nascent adhesions into focal adhesions. In this paper, we present a comprehensive proteomic analysis of nascent and mature adhesions. The purification of integrin adhesion complexes combined with quantitative mass spectrometry enabled the identification and quantification of known and new adhesion-associated proteins. Furthermore, blocking adhesion maturation with the myosin II inhibitor blebbistatin markedly impaired the recruitment of LIM domain proteins to integrin adhesion sites. This suggests a common recruitment mechanism for a whole class of adhesion-associated proteins, involving myosin II and the zinc-finger-type LIM domain.
整合素的一个特点是它们能够在质膜两侧传递化学和机械信号。肌球蛋白 II 产生的力使细胞能够感知基质硬度，并诱导新生黏附体成熟为黏附斑。在本文中，我们对新生和成熟黏附体进行了全面的蛋白质组学分析。通过将整合素黏附复合物与定量质谱相结合进行纯化，我们能够鉴定和定量已知和新的黏附相关蛋白。此外，用肌球蛋白 II 抑制剂 blebbistatin 阻断黏附体成熟显著削弱了 LIM 结构域蛋白向整合素黏附部位的募集。这表明整类黏附相关蛋白的募集机制相同，涉及肌球蛋白 II 和锌指型 LIM 结构域。
