期刊信息

  • 刊名: 河北师范大学学报(自然科学版)Journal of Hebei Normal University (Natural Science)
  • 主办: 河北师范大学
  • ISSN: 1000-5854
  • CN: 13-1061/N
  • 中国科技核心期刊
  • 中国期刊方阵入选期刊
  • 中国高校优秀科技期刊
  • 华北优秀期刊
  • 河北省优秀科技期刊

拟南芥CLAVATA3受体的研究进展

  • 河北化工医药职业技术学院 制药工程系, 河北 石家庄 050026
  • DOI: 10.11826/j.issn.1000-5854.2014.04.021

Research Progress of CLAVATA3 Receptors of Arabidopsis thaliana

摘要/Abstract

摘要:

多肽配基CLAVATA3(CLV3)和转录因子WUSCHEL(WUS)构成的反馈调控环路调节拟南芥茎顶端分生区干细胞增殖与分化间的平衡.以前大家基于遗传实验的证据推测,CLV1/CLV2通过胞外域二硫键的连接形成二聚体来应答CLV3信号.2010年Clark研究组发现CLV1能够与其同源蛋白BAM形成异源二聚体CLV1/BAM来参与CLV3信号传递.遗传学分析表明CLV1和CLV2/CORYNE(CRN)分属2条平行独立的信号转导通路来应答CLV3多肽信号.2010年中科院植物研究所林金星研究组通过萤火虫荧光素酶互补技术检测到CRN与CLV2相互作用,CRN和CLV1能够产生较弱的相互作用,CRN自身相互作用形成二聚体,并且CLV1,CLV2和CRN可以结合在一起形成1个复合体.Simon实验组利用荧光能量共振转移技术亦得到相同的实验结果.2010年Sawa研究组利用遗传和生化技术,发现Receptor-like Protein Kinase2(RPK2)以形成同源二聚体RPK2/RPK2的形式参与CLV3信号传递.随着蛋白质之间关系的深入研究,人们发现CLV3受体形式非常复杂,远远不是推测的CLV1/CLV1(BAM),CLV2/CRN和RPK2/RPK23种形式的受体模型所能全部涵盖的.

Abstract:

The balance between proliferation and differentiation of stem cell in shoot apical meristem (SAM) of Arabidopsis thaliana is regulated by the feedback regulatory loop between peptide ligand CLAVATA3 (CLV3) and transcription factor WUSCHEL (WUS).Previously,based on evidence from genetics experiments,it was believed that the CLV3 signaling was transmitted by the putative CLV1/CLV2 heterodimer.In 2010,Clark group found that CLV1 and its homolog BAM could form a CLV1/BAM heterodimer to perceive and transmit CLV3 signaling.The genetic analysis suggested that CLV1 and CLV2/CORYNE (CRN) act in parallel pathways to perceive and transmit CLV3 signaling.Using the firefly luciferase complementation imaging assay in 2010,Lin group found that CRN could interact with CLV2 and interact weakly with CLV1.They also discovered that CRN could form homodimers,and CRN could form a complex with CLV1 and CLV2.Simon group also got the same results using fluorescence resonance energy transfer assay.Combining genetic and biochemical evidence,Sawa group found in 2010 that receptor-like protein kinase2 (RPK2) could form a RPK2/RPK2 homodimer to transmit CLV3 signaling.As the study on protein-protein interactions deepened,we found the relationships among CLV3 receptors were much more complex than that indicated in the aforementioned three parallel pathway models.

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