Phospholipase C binds to the receptor-like GPR1 protein and controls pseudohyphal differentiation in Saccharomyces cerevisiae
Phospholipase C binds to the receptor-like GPR1 protein and controls pseudohyphal differentiation in Saccharomyces cerevisiae
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DOI：
10.1074/jbc.274.42.30052
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发表时间：
1999-10-15
影响因子：
4.8
通讯作者：
Küntzel, H
中科院分区：
文献类型：
--
作者：
Ansari, K;Martin, S;Küntzel, H
激素受体样蛋白Gpr 1 p与磷脂酰肌醇特异性磷脂酶C（Plc 1 p）和G α蛋白Gpa 2 p相互作用，如双杂交试验和表位标记蛋白的共免疫沉淀所示。Plc 1 p在Gpa 2存在或不存在的情况下与Gpr 1 p结合，而Gpr 1 p/Gpa 2 p结合依赖于Plc 1 p的存在。无效突变plc 1D、gpr 1D、gpa 2 δ和ras 2 δ之间的遗传相互作用表明Plc 1 p与Gpr 1 p和Gpa 2 p一起在生长控制途径中与ras 2 p功能平行地起作用，缺乏Gpr 1 p、Plc 1 p或Gpa 2 p的二倍体细胞在氮耗尽时不能形成假菌丝，并且gpr 1D和plc 1D菌株的表达缺陷通过经STE 11 -4激活促分裂原活化蛋白激酶途径或通过经过表达的Tpk 2 p激活cAMP途径来挽救，Plc 1 p也需要FG（TyA）：：lacZ报告基因在氮depletion.In结论，我们已经确定了两个物理相互作用的蛋白质，Gpr 1 p和Plc 1 p，作为一个新的组成部分的氮信号通路控制的发展开关从酵母样假菌丝生长。我们的数据表明，磷脂酶C调节的相互作用的假定的营养传感器Gpr 1 p与G α蛋白Gpa 2 p作为下游效应的抑制控制。
The hormone receptor-like protein Gpr1p physically interacts with phosphatidylinositol-specific phospholipase C (Plc1p) and with the G alpha protein Gpa2p, as shown by two-hybrid assays and co-immune precipitation of epitope-tagged proteins. Plc1p binds to Gpr1p in either the presence or absence of Gpa2, whereas the Gpr1p/Gpa2p association depends on the presence of Plc1p. Genetic interactions between the null mutations plc1D, gpr1D, gpa2 Delta, and ras2 Delta suggest that Plc1p acts together with Gpr1p and Gpa2p in a growth control pathway operating in parallel to the Ras2p function, Diploid cells lacking Gpr1p, Plc1p, or Gpa2p fail to form pseudohyphae upon nitrogen depletion, and the filamentation defect of gpr1D and plc1D strains is rescued by activating a mitogen-activated protein kinase pathway via STE11-4 or by activating a cAMP pathway via overexpressed Tpk2p, Plc1p is also required for efficient expression of the FG(TyA)::lacZ reporter gene under nitrogen depletion.In conclusion, we have identified two physically interacting proteins, Gpr1p and Plc1p, as novel components of a nitrogen signaling pathway controlling the developmental switch from yeast-like to pseudohyphal growth. Our data suggest that phospholipase C modulates the interaction of the putative nutrient sensor Gpr1p with the G alpha protein Gpa2p as a downstream effector of filamentation control.