Aspenström Pontus
Ludwig Institute for Cancer Research, Uppsala University, SE-751 24 Uppsala, Sweden.
Int Rev Cell Mol Biol. 2009;272:1-31. doi: 10.1016/S1937-6448(08)01601-8.
The Pombe Cdc15 Homology (PCH) proteins have emerged in many species as important coordinators of signaling pathways that regulate actomyosin assembly and membrane dynamics. The hallmark of the PCH proteins is the presence of a Fes/CIP4 homology-Bin/Amphiphysin/Rvsp (F-BAR) domain; therefore they are commonly referred to as F-BAR proteins. The prototype F-BAR protein, Cdc15p of Schizosaccharomyces pombe, has a role in the formation of the contractile actomyosin ring during cytokinesis. Vertebrate F-BAR proteins have an established role in binding phospholipids and they participate in membrane deformations, for instance, during the internalization of transmembrane receptors. This way the F-BAR proteins will function as linkers between the actin polymerization apparatus and the machinery regulating membrane dynamics. Interestingly, some members of the F-BAR proteins are implicated in inflammatory or neurodegenerative disorders and the observations can be expected to have clinical implications for the treatment of the diseases.
粟酒裂殖酵母Cdc15同源（PCH）蛋白在许多物种中已成为调节肌动球蛋白组装和膜动力学的信号通路的重要协调因子。PCH蛋白的标志是存在Fes/CIP4同源结构域-Bin/Amphiphysin/Rvsp（F-BAR）结构域；因此它们通常被称为F-BAR蛋白。F-BAR蛋白的原型，即粟酒裂殖酵母的Cdc15p，在胞质分裂过程中收缩性肌动球蛋白环的形成中发挥作用。脊椎动物的F-BAR蛋白在结合磷脂方面具有既定作用，并且它们参与膜变形，例如在跨膜受体的内化过程中。通过这种方式，F-BAR蛋白将作为肌动蛋白聚合装置与调节膜动力学的机制之间的连接物。有趣的是，一些F-BAR蛋白成员与炎症或神经退行性疾病有关，预计这些观察结果对这些疾病的治疗具有临床意义。
