Comparative phyloproteomics identifies conserved plasmodesmal proteins

Johnston, Matthew G.; Breakspear, Andrew; Samwald, Sebastian; Zhang, Dan; Papp, Diana; Faulkner, Christine; Keijzer, Jeroen de

doi:10.1101/2022.06.01.494363

Cited by 2 publications

(1 citation statement)

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“…Given that PDLP1 and PDLP5 interact (10) we propose they function in complex with NHL3, forming an integrator of immune signal inputs. PDLPs are only found in seed plants (24–28), indicating a recent emergence in comparison to NHL related proteins which have orthologues to proteins found in plasmodesmal fractions of the earlier land plant Physcomitrium patens (26, 29); this allows speculation that PDLPs were co-opted into a pre-existing complex of NHLs with callose synthases to enable an extra regulatory mechanism for plasmodesmata responses.…”

Section: Discussionmentioning

confidence: 99%

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

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Johnston

Papp

et al. 2022

Preprint

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The plant immune system relies on the perception of molecules that signal the presence of a microbe threat. This triggers signal transduction that mediates a range of cellular responses via a collection of molecular machinery including receptors, small molecules, and enzymes. One response to pathogen perception is the restriction of cell-to-cell communication by plasmodesmal closure. We previously found that while chitin and flg22 trigger specialized immune signaling cascades in the plasmodesmal plasma membrane, both execute plasmodesmal closure via callose synthesis at the plasmodesmata. This indicates the signaling pathways ultimately converge at or upstream of callose synthesis. To establish the hierarchy of signaling at plasmodesmata and characterize points of convergence in microbe elicitor-triggered signaling, we profiled the dependence of plasmodesmal responses triggered by different elicitors on a range of plasmodesmal signaling machinery. We identified that, like chitin, flg22 signals via RBOHD to induce plasmodesmal closure. Further, we found that PDLP1, PDLP5 and CALS1 are common to microbe- and SA-triggered responses, identifying PDLPs as a candidate signaling nexus. To understand how PDLPs relay a signal to CALS1, we screened for PDLP5 interactors and found NHL3, which is also required for chitin-, flg22- and SA-triggered plasmodesmal responses and PDLP-mediated activation of callose synthesis. We conclude that a PDLP-NHL3 complex acts as an integrating node of plasmodesmal signaling cascades, transmitting multiple immune signals to activate CALS1 and plasmodesmata closure.

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Section: Discussionmentioning

confidence: 99%

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

Tee

Johnston

Papp

et al. 2022

Preprint

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Do photosynthetic cells communicate with each other during cell death? From cyanobacteria to vascular plants

Aguilera

Distefano

Jauzein

et al. 2022

Journal of Experimental Botany

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As in metazoans, life in oxygenic photosynthetic organisms relies on the accurate regulation of cell death. During development and in response to the environment, photosynthetic cells activate and execute cell death pathways that culminate in the death of a specific group of cells, a process known as regulated cell death (RCD). RCD control is instrumental, as its mis regulation can lead to growth penalties and even the death of the entire organism. Intracellular molecules released during cell demise may act as “survival” or “death” signals and control the propagation of cell death to surrounding cells, even in unicellular organisms. This review explores different signals involved in cell-cell communication and systemic signaling in photosynthetic organisms, in particular Ca 2+, ROS, lipid derivates, NO and eATP. We discuss their possible mode-of-action as either “survival” and “death” molecules and their potential role in determining cell fate in neighboring cells. By comparing the knowledge available across the taxonomic spectrum of this coherent phylogenetic group, from cyanobacteria to vascular plants, we aim at contributing to the identification of conserved mechanisms that control cell death propagation in oxygenic photosynthetic organisms.

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Comparative phyloproteomics identifies conserved plasmodesmal proteins

Cited by 2 publications

References 88 publications

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

Do photosynthetic cells communicate with each other during cell death? From cyanobacteria to vascular plants

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