Kimmel Alan R, Parent Carole A
Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
Science. 2003 Jun 6;300(5625):1525-7. doi: 10.1126/science.1085439.
Cells migrating directionally toward a chemoattractant source display a highly polarized cytoskeletal organization, with F-actin localized predominantly at the anterior and myosin II at the lateral and posterior regions. Dictyostelium discoideum has proven a useful system for elucidating signaling pathways that regulate this chemotactic response. During development, extracellular adenosine 3', 5' monophosphate (cAMP) functions as a primary signal to activate cell surface cAMP receptors (cARs). These receptors transduce different signals depending on whether or not they are coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) (see the STKE Connections Maps). Multiple G protein-stimulated pathways interact to establish polarity in chemotaxing D. discoideum cells by localizing F-actin at their leading edge and by regulating the phosphorylation state and assembly of myosin II. Many of the molecular interactions described are fundamental to the regulation of chemotaxis in other eukaryotic cells.
细胞朝着趋化因子源定向迁移时,会呈现出高度极化的细胞骨架组织,其中F-肌动蛋白主要定位于前部,肌球蛋白II定位于侧面和后部区域。盘基网柄菌已被证明是阐明调节这种趋化反应信号通路的有用系统。在发育过程中,细胞外3',5'-环磷酸腺苷(cAMP)作为主要信号激活细胞表面的cAMP受体(cARs)。这些受体根据是否与异三聚体鸟嘌呤核苷酸结合蛋白(G蛋白)偶联而转导不同的信号(见STKE连接图谱)。多种G蛋白刺激的信号通路相互作用,通过将F-肌动蛋白定位在趋化盘基网柄菌细胞的前缘,并调节肌球蛋白II的磷酸化状态和组装,从而建立极性。所描述的许多分子相互作用对于其他真核细胞趋化性的调节至关重要。