Hurley J H, Misra S
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA.
Annu Rev Biophys Biomol Struct. 2000;29:49-79. doi: 10.1146/annurev.biophys.29.1.49.
Protein kinase C homology-1 and -2, FYVE, and pleckstrin homology domains are ubiquitous in eukaryotic signal transduction and membrane-trafficking proteins. These domains regulate subcellular localization and protein function by binding to lipid ligands embedded in cell membranes. Structural and biochemical analysis of these domains has shown that their molecular mechanisms of membrane binding depend on a combination of specific and nonspecific interactions with membrane lipids. In vivo studies of green fluorescent protein fusions have highlighted the key roles of these domains in regulating protein localization to plasma and internal membranes in cells.
蛋白激酶C同源结构域1和2、FYVE结构域以及普列克底物蛋白同源结构域在真核生物信号转导和膜运输蛋白中普遍存在。这些结构域通过与嵌入细胞膜的脂质配体结合来调节亚细胞定位和蛋白质功能。对这些结构域的结构和生化分析表明，它们与膜结合的分子机制取决于与膜脂的特异性和非特异性相互作用的组合。绿色荧光蛋白融合体的体内研究突出了这些结构域在调节蛋白质在细胞内质膜和质膜上定位中的关键作用。
