The putative G protein-coupled receptor GrlD mediates extracellular polyphosphate sensing in Dictyostelium discoideum.
The putative G protein-coupled receptor GrlD mediates extracellular polyphosphate sensing in Dictyostelium discoideum.
复制标题
盘基网柄菌中假定的 G 蛋白偶联受体 GrlD 介导细胞外多磷酸盐传感。
DOI:
10.1091/mbc.e18-10-0686
复制
发表时间:
2019
影响因子:
3.3
通讯作者:
Gomer,RichardH
中科院分区:
文献类型:
--
作者:
Suess,PatrickM;Tang,Yu;Gomer,RichardH
Five or more orthophosphates bound together by high-energy phosphoanhydride bonds are highly ubiquitous inorganic molecules called polyphosphate. Polyphosphate acts as a signaling molecule eliciting a number of responses in eukaryotic cells, but the mechanisms mediating these effects are poorly understood. ProliferatingDictyostelium discoideumcells accumulate extracellular polyphosphate. At extracellular concentrations similar to those observed in stationary phase cells, polyphosphate inhibits proteasome activity and proliferation, and induces aggregation. Here we identify GrlD as a putative G protein–coupled receptor that mediates binding of extracellular polyphosphate to the cell surface. Cells lacking GrlD do not respond to polyphosphate-induced proteasome inhibition, aggregation, or proliferation inhibition. Polyphosphate also elicits differential effects on cell-substratum adhesion and cytoskeletal F-actin levels based on nutrient availability, and these effects were also mediated by GrlD. Starving cells also accumulate extracellular polyphosphate. Starved cells treated with exopolyphosphatase failed to aggregate effectively, suggesting that polyphosphate also acts as a signaling molecule during starvation-induced development ofDictyostelium. Together, these results suggest that a eukaryotic cell uses a G protein–coupled receptor to mediate the sensing and response to extracellular polyphosphate.