The higher plant peptide hormone CLAVATA3 (CLV3) plays an extremely important role in maintaining the number of stem stem meristem stem cells. Over the past few decades, the CLAVATA1 / CLAVATA2 (CLV1 / CLV2) complex is considered to be the sole receptor for CLV3 polypeptides on the cell membrane. However, a recent genetic analysis has screened a new receptor protein kinase member, CORYNE (CRN), and found that it plays a very important role in the CLV3 signaling pathway. On the basis of a series of genetic analysis, the new CLV3 signal transduction pathway hypothesis was proposed: that CLV1 homodimer and CLV2 / CRN heterologous complex may mediate CLV3 signal independently in parallel. However, the new hypothesis only stays on genetic predictions, and there is still a lack of further biochemical and cytological evidence. In order to better understand the relationship between these three possible receptor proteins, Lin Jinxing's team used a new in vivo technique to detect protein interactions-Firefly luciferase complementation imaging assay (LCI) The interaction between the three receptor proteins CLV1, CLV2 and CRN was analyzed in two systems of Arabidopsis mesophyll protoplasts and Nicotiana benthamiana leaves. The experimental results show that: LCI technology and Co-immunoprecipitation assay both confirm that CLV2 can directly interact with CRN without the stimulation of CLV3 polypeptide; the treatment of exogenous CLV3 polypeptide does not significantly Affect the strength of the interaction between CLV2-CRN; further LCI experiments found that CLV1 cannot directly interact with CLV2, but can interact weakly with CRN; in addition, the experimenters also found that CRN itself can form Homodimers, and CLV1 or CLV2 cannot form homodimers by themselves. These biochemical and cytological results provide direct evidence for the newly proposed CLV3 parallel dual pathway hypothesis.
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