The maize Gα gene COMPACT PLANT2 functions in CLAVATA signalling to control shoot meristem size

The maize Gα gene COMPACT PLANT2 functions in CLAVATA signalling to control shoot meristem size
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DOI:
10.1038/nature12583
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发表时间:
2013-10-24
期刊:
影响因子:
64.8
通讯作者:
Jackson, David
Jackson, David
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Bommert, Peter;Il Je, Byoung;Jackson, David

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芽生长依赖于分生组织,由CLAVATA途径和WUSCHEL同源框基因之间的负反馈回路维持的干细胞池(1)。CLAVATA信号传导涉及一种分泌肽CLAVATA 3(CLV 3)(2)及其被细胞表面富亮氨酸重复序列(LRR)受体感知,包括CLV 1受体激酶(3)和LRR受体样蛋白CLV 2(参考文献4)。然而,对这些受体下游的信号传导机制知之甚少,特别是缺乏信号传导结构域的LRR受体样蛋白(5)。在这里,我们表明,玉米COMPACT PLANT 2(CT 2)编码预测的α亚基(G α)的异源三聚体GTP结合蛋白。玉米ct 2表型类似于拟南芥棒突变体,遗传,生化和功能测定表明,CT 2/G α传递干细胞限制性信号从CLAVATA LRR受体,这表明一个新的功能,G α信号在植物中。异三聚体GP结合蛋白是膜相关分子开关,通常通过配体与相关七次跨膜(7 TM)G蛋白偶联受体(GPCR)结合而激活(6)。最近的研究质疑了植物异源三聚体G蛋白与典型GPCR相互作用的观点(7),我们的研究结果表明,单次跨膜受体在植物中充当GPCR,挑战了GPCR仅是7 TM蛋白的教条。
Shoot growth depends on meristems, pools of stem cells that are maintained by a negative feedback loop between the CLAVATA pathway and the WUSCHEL homeobox gene(1). CLAVATA signalling involves a secreted peptide, CLAVATA3 (CLV3)(2), and its perception by cell surface leucine-rich repeat (LRR) receptors, including the CLV1 receptor kinase(3) and a LRR receptor-like protein, CLV2 (ref. 4). However, the signalling mechanisms downstream of these receptors are poorly understood, especially for LRR receptor-like proteins, which lack a signalling domain(5). Here we show that maize COMPACT PLANT2 (CT2) encodes the predicted alpha-subunit (G alpha) of a heterotrimeric GTP binding protein. Maize ct2 phenotypes resemble Arabidopsis thaliana clavata mutants, and genetic, biochemical and functional assays indicate that CT2/G alpha transmits a stem-cell-restrictive signal from a CLAVATA LRR receptor, suggesting a new function for G alpha signalling in plants. Heterotrimeric GTP-binding proteins are membrane-associated molecular switches that are commonly activated by ligand binding to an associated seven-pass transmembrane (7TM) G-protein-coupled receptor (GPCR)(6). Recent studies have questioned the idea that plant heterotrimeric G proteins interact with canonical GPCRs(7), and our findings suggest that single pass transmembrane receptors act as GPCRs in plants, challenging the dogma that GPCRs are exclusively 7TM proteins.