Goα regulates olfactory adaptation by antagonizing Gqα-DAG signaling in Caenorhabditis elegans
Goα regulates olfactory adaptation by antagonizing Gqα-DAG signaling in Caenorhabditis elegans
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DOI：
10.1073/pnas.0506954103
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发表时间：
2006-01-24
影响因子：
11.1
通讯作者：
Iino, Y
中科院分区：
文献类型：
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作者：
Matsuki, M;Kunitomo, H;Iino, Y
异源三聚体G蛋白Go在哺乳动物神经系统中大量表达，并响应于各种配体调节神经活动。然而，Go在活体动物中的功能还不太清楚。在这里，我们证明了果阿-1 G（o）α在秀丽隐杆线虫的嗅觉适应中具有重要作用。果阿-1 G（o）α功能的损害和EGL-30 G（q）α的过度活化导致对AWC感知的气味剂的适应缺陷。这些通路拮抗性地调节AWC化学感觉神经元的嗅觉适应。用佛波醇酯处理的野生型动物和二酰基甘油（DAG）激酶dgk-3; dgk-1的双突变动物也具有适应缺陷，表明升高的DAG信号破坏正常适应。组成型活性果阿1可抑制dgk-3、dgk-1双突变体的适应缺陷，而不能抑制具有组成型活性EGL-30的动物的适应缺陷，这意味着果阿1在嗅觉适应中作用于EGL-30的上游。我们的研究结果表明，EGL-30-DAG信号的下调果阿-1的基础嗅觉适应和可塑性的趋化性。
The heterotrimeric G protein Go is abundantly expressed in the mammalian nervous system and modulates neural activities in response to various ligands. However, Go's functions in living animals are less well understood. Here, we demonstrate that GOA-1 G(o)alpha has a fundamental role in olfactory adaptation in Caenorhabditis elegans. Impairment of GOA-1 G(o)alpha function and excessive activation of EGL-30 G(q)alpha cause a defect in adaptation to AWC-sensed odorants. These pathways antagonistically modulate olfactory adaptation in AWC chemosensory neurons. Wild-type animals treated with phorbol esters and double-mutant animals of diacylglycerol (DAG) kinases, dgk-3; dgk-1, also have a defect in adaptation, suggesting that elevated DAG signals disrupt normal adaptation. Constitutively active GOA-1 can suppress the adaptation, defect of dgk-3; dgk-1 double mutants, whereas it fails to suppress the adaptation defect of animals with constitutively active EGL-30, implying that GOA-1 acts upstream of EGL-30 in olfactory adaptation. Our results suggest that down-regulation of EGL-30-DAG signaling by GOA-1 underlies olfactory adaptation and plasticity of chemotaxis.