Comparative phyloproteomics identifies conserved plasmodesmal proteins

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

doi:10.1093/jxb/erad022

Cited by 9 publications

(11 citation statements)

References 70 publications

(93 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This points to a functional diversification of PD and non-PD-localized members of the GHL17 family or that only PD-localized PpGHL17s can degrade callose at PD. In recent parallel work, GHL17_4 (Pp3c11_25840) and GHL17_18 (Ppc16_15860), also members of the GHL17 alpha clade, were localized to PD in P. patens (Johnston et al, 2023), thus adding further evidence for PD localization of alpha clade GHL17s.…”

Section: Phylogenetic Distribution Of Glycosyl Hydrolase Family 17mentioning

confidence: 84%

A high‐confidence Physcomitrium patens plasmodesmata proteome by iterative scoring and validation reveals diversification of cell wall proteins during evolution

et al. 2023

View full text Add to dashboard Cite

Summary Plasmodesmata (PD) facilitate movement of molecules between plant cells. Regulation of this movement is still not understood. Plasmodesmata are hard to study, being deeply embedded within cell walls and incorporating several membrane types. Thus, structure and protein composition of PD remain enigmatic. Previous studies of PD protein composition identified protein lists with few validations, making functional conclusions difficult. We developed a PD scoring approach in iteration with large‐scale systematic localization, defining a high‐confidence PD proteome of Physcomitrium patens (HC300). HC300, together with bona fide PD proteins from literature, were placed in Pddb. About 65% of proteins in HC300 were not previously PD‐localized. Callose‐degrading glycolyl hydrolase family 17 (GHL17) is an abundant protein family with representatives across evolutionary scale. Among GHL17s, we exclusively found members of one phylogenetic clade with PD localization and orthologs occur only in species with developed PD. Phylogenetic comparison was expanded to xyloglucan endotransglucosylases/hydrolases and Exordium‐like proteins, which also diversified into PD‐localized and non‐PD‐localized members on distinct phylogenetic clades. Our high‐confidence PD proteome HC300 provides insights into diversification of large protein families. Iterative and systematic large‐scale localization across plant species strengthens the reliability of HC300 as basis for exploring structure, function, and evolution of this important organelle.

show abstract

Section: Phylogenetic Distribution Of Glycosyl Hydrolase Family 17mentioning

confidence: 84%

A high‐confidence Physcomitrium patens plasmodesmata proteome by iterative scoring and validation reveals diversification of cell wall proteins during evolution

et al. 2023

View full text Add to dashboard Cite

show abstract

“…Their meristems have a simpler organization while at the same time still sharing genetic control elements with higher plants [ 141 ]. Furthermore, knowledge of the molecular makeup of bryophyte plasmodesmata is emerging, along with tools for studying plasmodesmal function [ 67 , 142 , 143 ]. Beyond the advantages in terms of a more accessible body plan, the inclusion of bryophytes could shed an evo-devo light on the control mechanisms for mobile developmental regulators.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, live-cell, light-based fluorescence microscopy with higher resolving power in combination with markers that distinguish plasmodesmal morphology type could be a promising approach. The expanding knowledge of protein presence at different plasmodesmata via proteomics could provide candidates for such markers [ 67 ].…”

Section: Setting the Stage For Intercellular Transport: Biogenesis An...mentioning

confidence: 99%

Distributing Plant Developmental Regulatory Proteins via Plasmodesmata

Schreiber,

Limpens,

de Keijzer

2024

Plants

Self Cite

View full text Add to dashboard Cite

During plant development, mobile proteins, including transcription factors, abundantly serve as messengers between cells to activate transcriptional signaling cascades in distal tissues. These proteins travel from cell to cell via nanoscopic tunnels in the cell wall known as plasmodesmata. Cellular control over this intercellular movement can occur at two likely interdependent levels. It involves regulation at the level of plasmodesmata density and structure as well as at the level of the cargo proteins that traverse these tunnels. In this review, we cover the dynamics of plasmodesmata formation and structure in a developmental context together with recent insights into the mechanisms that may control these aspects. Furthermore, we explore the processes involved in cargo-specific mechanisms that control the transport of proteins via plasmodesmata. Instead of a one-fits-all mechanism, a pluriform repertoire of mechanisms is encountered that controls the intercellular transport of proteins via plasmodesmata to control plant development.

show abstract

“…S11 ). Irrespective of the working model, PDLPs are only found in seed plants ( 28 – 32 ), while NHL-related proteins have orthologues the earlier land plant Physcomitrium patens ( 30 , 33 ). This allows speculation that PDLPs were co-opted into a preexisting complex of NHLs that activates callose synthases to enable an extra regulatory mechanism for plasmodesmata responses.…”

Section: Discussionmentioning

confidence: 99%

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

Tee

Johnston

Papp

et al. 2023

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

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. Therefore, 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 RESPIRATORY BURST OXIDASE HOMOLOGUE D (RBOHD) to induce plasmodesmal closure. Further, we found that PLASMODESMATA-LOCATED PROTEIN 1 (PDLP1), PDLP5, and CALLOSE SYNTHASE 1 (CALS1) are common to microbe- and salicylic acid (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 NON-RACE SPECIFIC DISEASE RESISTANCE/HIN1 HAIRPIN-INDUCED-LIKE protein 3 (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.

show abstract

Comparative phyloproteomics identifies conserved plasmodesmal proteins

Cited by 9 publications

References 70 publications

A high‐confidence Physcomitrium patens plasmodesmata proteome by iterative scoring and validation reveals diversification of cell wall proteins during evolution

A high‐confidence Physcomitrium patens plasmodesmata proteome by iterative scoring and validation reveals diversification of cell wall proteins during evolution

Distributing Plant Developmental Regulatory Proteins via Plasmodesmata

A PDLP-NHL3 complex integrates plasmodesmal immune signaling cascades

Contact Info

Product

Resources

About