The Role of Plasmodesmata-Associated Receptor in Plant Development and Environmental Response

Vu, Minh Huy; Iswanto, Arya Bagus Boedi; Lee, Jinsu; Kim, Jae Yean

doi:10.3390/plants9020216

Cited by 20 publications

(17 citation statements)

References 110 publications

(154 reference statements)

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“…PDLP5 is highly accumulated in the leaf epidermal cells of sld1 sld2 double mutant where trihydroxy LCB or phytosphinganine t18:0 is elevated. Similarly, PDLP5 overexpression plant and sld1 sld2 double mutant show decreased PD permeability through callose accumulation (Chen et al, 2012; Wang et al, 2013; Liu et al, 2020; Vu et al, 2020). However, GlcCers proportions are strongly attenuated in the sld1 sld2 double mutant (Chen et al, 2012), led us to speculate that GlcHCers might also be impaired.…”

Section: Discussionmentioning

confidence: 98%

Glucosylhydroxyceramides Modulate Secretion Machinery of a Subset of Plasmodesmata Proteins and a Change in the Callose Accumulation

Iswanto

Shon

et al. 2020

Preprint

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The plasma membranes encapsulated in the plasmodesmata (PDs) with symplasmic nano-channels contain abundant lipid rafts, which are enriched by sphingolipids and sterols. The attenuation of sterol compositions has demonstrated the role played by lipid raft integrity in the intercellular trafficking of glycosylphosphatidylinositol (GPI)-anchored PD proteins, particularly affecting in the callose enhancement. The presence of callose at PD is tightly attributed to the callose metabolic enzymes, callose synthases (CalSs) and β-1,3-glucanases (BGs) in regulating callose accumulation and callose degradation, respectively. Sphingolipids have been implicated in signaling and membrane protein trafficking, however the underlying processes linking sphingolipid compositions to the control of symplasmic apertures remain unknown. A wide variety of sphingolipids in plants prompts us to investigate which sphingolipid molecules are important in regulating symplasmic apertures. Here, we demonstrate that perturbations of sphingolipid metabolism by introducing several potential sphingolipid (SL) pathway inhibitors and genetically modifying SL contents from two independent SL pathway mutants are able to modulate callose deposition to control symplasmic connectivity. Our data from pharmacological and genetic approaches show that the alteration in glucosylhydroxyceramides (GlcHCers) particularly disturb the secretory machinery for GPI-anchored PdBG2 protein, resulting in an over accumulated callose. Moreover, our results reveal that SL-enriched lipid rafts link symplasmic channeling to PD callose homeostasis by controlling the targeting of GPI-anchored PdBG2. This study elevates our understanding of the molecular linkage underlying intracellular trafficking and precise targeting to specific destination of GPI-anchored PD proteins incorporated with GlcHCers contents.

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Section: Discussionmentioning

confidence: 98%

Glucosylhydroxyceramides Modulate Secretion Machinery of a Subset of Plasmodesmata Proteins and a Change in the Callose Accumulation

Iswanto

Shon

et al. 2020

Preprint

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“…The diameters area of necrotic lesion in α1-cop-1 and α1-cop-5 mutants were significantly larger than in wild-type Col-0 and α1-COP overexpression plants (Figure 11A, B) . In the previous study, a PD receptor-like protein, named LYSIN MOTIF DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED PROTEIN 2 (LYM2) is suggested to be an essential factor during B. cinerea infection in Arabidopsis (Faulkner et al, 2013; Vu et al, 2020). Since α1-COP is required for the proper intracellular trafficking of GPI-anchored PdBG2, we hypothesize that α1-COP is presumably associated with GPI-anchored LYM2 functioning.…”

Section: Resultsmentioning

confidence: 99%

α1-COP delivers sphingolipid modifiers and controls plasmodesmal callose deposition in Arabidopsis

Iswanto

Kumar

et al. 2021

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Callose is a plant cell wall polymer in the form of β-1,3-glucan, which regulates symplasmic channel size at plasmodesmata (PD). It plays a crucial role in a variety of processes in plants through the regulation of intercelluar symplasmic continuity. However, how to maintain callose homeostasis at PD in the molecular levels is poorly understood. To further elucidate the mechanism of PD callose homeostasis, we screened and identified an Arabidopsis mutant plant that exhibited excessive callose deposition at PD. Based on the Next-generation sequencing (NGS)-based mapping, other mutant allele analysis, and complementation assay, the mutated gene was shown to be α1-COP, which encodes a member of the COPI coatomer complex comprised of α, β, β′, γ, δ, ε, and ζ subunits. Since there is no report on the link between COPI and callose/PD, it was extremely curious to know the roles of α1-COP or COPI in PD regulation through callose deposition. Here, we report that loss-of-function of α1-COP directly elevates the callose accumulation at PD by affecting subcellular protein localization of callose degradation enzyme PdBG2. This process is linked to ERH1, an inositol phosphoryl ceramide synthase (IPCS), and glucosylceramide synthase (GCS) functions through physical interactions with the α1-COP protein. In addition, the loss-of-function of α1-COP also alters the subcellular localization of ERH1 and GCS proteins, results in a reduction of GlcCers and GlcHCers molecules, which are the key SL species for lipid raft formation. According to our findings, we propose that α1-COP protein, together with the SL modifiers controlling lipid raft compositions, regulates the function of GPI-anchored PD proteins and hence the callose turnover at PD and symplastic movement of biomolecules. Our findings provide the first key clue to link the COPI-mediated intracellular trafficking pathway to the callose-mediated intercellular signaling pathway through PD.

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“…Many aspects of PD function and regulation are not well understood despite the increasing evidence of the important role these structures play in plant signalling, organ development and response to physiological and environmental cues (Petit et al, 2020;Vu et al, 2020;Li et al, 2021). Proteomic data is lacking for most plant species due to difficulties in isolating clean PD fractions and because association to PD domains can be quite dynamic, varying with environmental conditions and tissue types (Grison et al, 2019;Hunter et al, 2019;Cheval et al, 2020).…”

Section: Discussionmentioning

confidence: 99%

Comparative meta-proteomic analysis for the identification of novel plasmodesmata proteins and regulatory cues

Kirk

Amsbury

German

et al. 2021

Preprint

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SummaryA major route for cell-to-cell signaling is via cell wall-embedded pores termed plasmodesmata (PD). PD regulate many aspects of plant development and responses to the environment however, our understanding of what factors affect their structure and permeability is limited. In this paper, a meta-analysis is presented as a tool for the identification of conditions affecting PD transport and generation of PD proteomes in species in which experimental data is not available. A custom-built pipeline was developed to rapidly generate candidate PD proteomes for species of interest. The pipeline uses protein structural features and conserved domains to predict and prioritize validation of PD candidate proteins. Co-expression tables generated using published microarrays identify putative interactions between PD genes and conditions affecting PD function. We provide evidence that high salinity and osmotic stress regulate the expression of PD candidate proteins and symplasmic phloem unloading of GFP. The PD proteome for Medicago truncatula was generated in silico leading to the identification and experimental determination of a receptor like protein that target PD in root cortical cells. Together the results highlight the power of our newly designed tool in the identification of new factors and proteins influencing PD in diverse plant species.

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The Role of Plasmodesmata-Associated Receptor in Plant Development and Environmental Response

Cited by 20 publications

References 110 publications

Glucosylhydroxyceramides Modulate Secretion Machinery of a Subset of Plasmodesmata Proteins and a Change in the Callose Accumulation

Glucosylhydroxyceramides Modulate Secretion Machinery of a Subset of Plasmodesmata Proteins and a Change in the Callose Accumulation

α1-COP delivers sphingolipid modifiers and controls plasmodesmal callose deposition in Arabidopsis

Comparative meta-proteomic analysis for the identification of novel plasmodesmata proteins and regulatory cues

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