Liqiang Dai
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Liqiang Dai has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
- Erxu Pi
College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 311121, China
1 shared publication - Jinbo Shen
Zhejiang A&F University
1 shared publication - Kedi Jiang
College of Life and Environmental Sciences, Hangzhou Normal University , Hangzhou
1 shared publication - Lihui Duan
College of Life and Environmental Sciences, Hangzhou Normal University , Hangzhou
1 shared publication - Liqun Du
Laboratory of Molecular Plant Science, Department of Horticulture, Washington State University, Pullman, WA 99164-6414, USA; College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang 310036, China
1 shared publication - Qian Guo
College of Life and Environmental Sciences, Hangzhou Normal University , Hangzhou
1 shared publication
Latest Publications
- 9 June 2026
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 202 (2)
Autophosphorylation at the C-terminus of the DMI3 calmodulin-binding domain dismantles CaM-DMI3-IPD3 to initiate root nodulation
The calcium/calmodulin-dependent protein kinase (CCaMK) DMI3 (Doesn't Make Infections 3) decodes rhizobia-induced Ca2+ signals through phosphorylation of its interacting partner, IPD3, thereby initiating root nodule symbiosis (RNS). However, the precise mechanism by which DMI3 activates this pathway remains unclear. Here, we show that phosphorylation of a triplet motif (S343S344T345) located at the C-terminus of the calmodulin-binding domain acts as a molecular switch. We identified T345 as a phosphorylation site that exhibits regulatory functions similar to those of S343 and S344. Phosphomimic mutations at any single residue of the 3 sites blocked DMI3-dependent nodulation, indicating that the kinase must initially remain nonphosphorylated at these positions. Conversely, simultaneous phosphorylation of at least 2 residues was required for symbiotic activity, revealing a transition from a phosphorylation-free state to a hyperphosphorylated status (simultaneous phosphorylation of at least 2 residues) at these sites. Phosphomimic mutations within the triplet enhanced DMI3 autophosphorylation (auto-P) but severely impaired its interaction with Ca2+/CaM and IPD3. In addition, the physical interaction between DMI3 and IPD3 suppressed IPD3-triggered MtNIN transcription and nodulation, indicating that DMI3 also acts as a negative regulator by sequestering activated IPD3. Thus, we propose a model in which repeated auto-P at the triplet contributes to RNS activation by dissociating the CaM-DMI3-IPD3 complex, thereby releasing phosphorylated and activated IPD3 to initiate the downstream transcriptional cascade. Our findings uncover a dual role for DMI3—as both a kinase and a scaffold—and clarify how auto-P within the triplet motif licenses IPD3 to trigger RNS.
- 9 June 2026
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 202 (2)
Autophosphorylation at the C-terminus of the DMI3 calmodulin-binding domain dismantles CaM-DMI3-IPD3 to initiate root nodulation
The calcium/calmodulin-dependent protein kinase (CCaMK) DMI3 (Doesn't Make Infections 3) decodes rhizobia-induced Ca2+ signals through phosphorylation of its interacting partner, IPD3, thereby initiating root nodule symbiosis (RNS). However, the precise mechanism by which DMI3 activates this pathway remains unclear. Here, we show that phosphorylation of a triplet motif (S343S344T345) located at the C-terminus of the calmodulin-binding domain acts as a molecular switch. We identified T345 as a phosphorylation site that exhibits regulatory functions similar to those of S343 and S344. Phosphomimic mutations at any single residue of the 3 sites blocked DMI3-dependent nodulation, indicating that the kinase must initially remain nonphosphorylated at these positions. Conversely, simultaneous phosphorylation of at least 2 residues was required for symbiotic activity, revealing a transition from a phosphorylation-free state to a hyperphosphorylated status (simultaneous phosphorylation of at least 2 residues) at these sites. Phosphomimic mutations within the triplet enhanced DMI3 autophosphorylation (auto-P) but severely impaired its interaction with Ca2+/CaM and IPD3. In addition, the physical interaction between DMI3 and IPD3 suppressed IPD3-triggered MtNIN transcription and nodulation, indicating that DMI3 also acts as a negative regulator by sequestering activated IPD3. Thus, we propose a model in which repeated auto-P at the triplet contributes to RNS activation by dissociating the CaM-DMI3-IPD3 complex, thereby releasing phosphorylated and activated IPD3 to initiate the downstream transcriptional cascade. Our findings uncover a dual role for DMI3—as both a kinase and a scaffold—and clarify how auto-P within the triplet motif licenses IPD3 to trigger RNS.