2. Academic Validation
  3. ER-PM tether Syt1 limits cell-to-cell connectivity via plasmodesmata during innate immune responses in Arabidopsis

ER-PM tether Syt1 limits cell-to-cell connectivity via plasmodesmata during innate immune responses in Arabidopsis

  • Cell Rep. 2025 May 27;44(5):115672. doi: 10.1016/j.celrep.2025.115672.
Jiajing Li 1,  Pengfei Lu 2,  Qing Pan 2,  Bingxiao Wang 2,  Youjun Wang 3,  Jiejie Li 4
Affiliations

Affiliations

  • 1 Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Science, Beijing Normal University, Beijing 100875, China; Guangdong Institute of Intelligence Science and Technology, Hengqin, Zhuhai 519031, China.
  • 2 Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Science, Beijing Normal University, Beijing 100875, China.
  • 3 Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Science, Beijing Normal University, Beijing 100875, China; Key Laboratory of Cell Proliferation and Regulation of Ministry of Education, College of Life Science, Beijing Normal University, Beijing 100875, China.
  • 4 Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Science, Beijing Normal University, Beijing 100875, China; Key Laboratory of Cell Proliferation and Regulation of Ministry of Education, College of Life Science, Beijing Normal University, Beijing 100875, China. Electronic address: jiejieli@bnu.edu.cn.
PMID: 40319474 DOI: 10.1016/j.celrep.2025.115672
Abstract

Upon perception of microbe-associated molecular patterns (MAMPs), Plants close plasmodesmata (PD) as part of their innate immune responses. However, the signaling cascades and molecular mechanisms underlying MAMP-induced PD closure require further investigation. Here, we show that the endoplasmic reticulum (ER)-plasma membrane (PM) tether Synaptotagmin 1 (Syt1) modulates the response of PD to MAMPs. Following MAMP stimulation, Syt1 rapidly accumulates to PD and further recruits a putative calcium-permeable transporter, ANN4, to promote a localized, PD-associated CA2+ elevation, leading to callose-dependent PD closure. Moreover, Syt1 can sense the increased level of PI(4,5)P2 at the PD-PM via its C2 domain. Disrupting the interaction between Syt1 and PM lipids by pharmaceutical approaches or site-directed mutagenesis leads to impaired PD response to MAMPs. Collectively, our findings reveal that Syt1 integrates phospholipid signaling from the PD-PM to regulate PD-localized CA2+ elevation, thereby modulating intercellular communication for restricting the spread of Bacterial infection.

Keywords

CP: Cell biology; CP: Plants; ER-PM contact sites; plant innate immunity; plasmodesmata; symplasmic trafficking; synaptotagmin.

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