Pribic Jelena, Garcia Rebecca, Kong May, Brazill Derrick
Department of Biological Sciences, Hunter College, 695 Park Avenue, New York, NY 10065, USA.
Eukaryot Cell. 2011 Jul;10(7):977-84. doi: 10.1128/EC.00282-10. Epub 2011 Apr 29.
The actin cytoskeleton forms a membrane-associated network whose proper regulation is essential for numerous processes, including cell differentiation, proliferation, adhesion, chemotaxis, endocytosis, exocytosis, and multicellular development. In this report, we show that in Dictyostelium discoideum, paxillin (PaxB) and phospholipase D (PldB) colocalize and coimmunoprecipitate, suggesting that they interact physically. Additionally, the phenotypes observed during development, cell sorting, and several actin-required processes, including cyclic AMP (cAMP) chemotaxis, cell-substrate adhesion, actin polymerization, phagocytosis, and exocytosis, reveal a genetic interaction between paxB and pldB, suggesting a functional interaction between their gene products. Taken together, our data point to PldB being a required binding partner of PaxB during processes involving actin reorganization.
肌动蛋白细胞骨架形成一个与膜相关的网络，其正常调节对于众多过程至关重要，包括细胞分化、增殖、黏附、趋化性、内吞作用、外排作用和多细胞发育。在本报告中，我们表明在盘基网柄菌中，桩蛋白（PaxB）和磷脂酶D（PldB）共定位且能进行共免疫沉淀，这表明它们在物理上相互作用。此外，在发育、细胞分选以及几个肌动蛋白依赖的过程中观察到的表型，包括环磷酸腺苷（cAMP）趋化性、细胞与底物的黏附、肌动蛋白聚合、吞噬作用和外排作用，揭示了paxB和pldB之间的遗传相互作用，表明它们的基因产物之间存在功能相互作用。综上所述，我们的数据表明在涉及肌动蛋白重组的过程中，PldB是PaxB必需的结合伴侣。
