Department of Physics, Biophysics Group, Friedrich-Alexander-University Erlangen-Nuremberg, D-91052, Erlangen, Germany.
Cell Biol Int. 2018 Aug;42(8):1076-1078. doi: 10.1002/cbin.10978. Epub 2018 May 22.
The focal adhesion protein vinculin has been implicated in associating with soluble and membranous phospholipids. Detailed investigations over the past ten years describe the intermolecular interactions of the vinculin tail domain with soluble and membrane phospholipids. Previous studies have implied that the tail's unstructured C-terminal region affects the mechanical behavior of cells and that the same region, at the molecular level, has bi-stable behavior sensitive to different protonation states. The aim of this short communication is to discuss whether the C-terminal vinculin tail (Vt) domain interacts favorably with membrane-embedded phospholipids such as PIP and that the region is also an anchor for lipid membranes.
粘着斑蛋白 vinculin 已被牵涉到与可溶性和膜磷脂的结合。在过去的十年中，详细的研究描述了 vinculin 尾部结构域与可溶性和膜磷脂的分子间相互作用。以前的研究表明，尾部的无规卷曲 C 端区域会影响细胞的力学行为，而同一区域在分子水平上具有对不同质子化状态敏感的双稳态行为。本短文的目的是讨论 vinculin 尾部（Vt）域是否与膜嵌入磷脂（如 PIP）有利相互作用，以及该区域是否也是脂质膜的锚点。
