Lipid Raft, Regulator of Plasmodesmal Callose Homeostasis

Iswanto, Arya Bagus Boedi; Kim, Jae‐Yean

doi:10.3390/plants6020015

Cited by 31 publications

(33 citation statements)

References 85 publications

(118 reference statements)

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“…The lipid composition of PDs is enriched in sterols and sphingolipids with very long chain saturated fatty acids (Grison et al 2015). This is reminiscent of DRMs and, consistent with this finding, members of the Remorin family and GAPs that are enriched in DRMs locate to PD (Raffaele et al 2009;Fernandez-Calvino et al 2011;Iswanto and Kim 2017).…”

Section: Association Of Gaps With Plasmodesmata In a Lipid-dependent supporting

confidence: 73%

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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Approximately 1% of plant proteins are predicted to be post-translationally modified with a glycosylphosphatidylinositol (GPI) anchor that tethers the polypeptide to the outer leaflet of the plasma membrane. Whereas the synthesis and structure of GPI anchors is largely conserved across eukaryotes, the repertoire of functional domains present in the GPI-anchored proteome has diverged substantially. In plants, this includes a large fraction of the GPI-anchored proteome being further modified with plant-specific arabinogalactan (AG) O-glycans. The importance of the GPI-anchored proteome to plant development is underscored by the fact that GPI biosynthetic null mutants exhibit embryo lethality. Mutations in genes encoding specific GPI-anchored proteins (GAPs) further supports their contribution to diverse biological processes, occurring at the interface of the plasma membrane and cell wall, including signaling, cell wall metabolism, cell wall polymer cross-linking, and plasmodesmatal transport. Here, we review the literature concerning plant GPI-anchored proteins, in the context of their potential to act as molecular hubs that mediate interactions between the plasma membrane and the cell wall, and their potential to transduce the signal into the protoplast and, thereby, activate signal transduction pathways.

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Section: Association Of Gaps With Plasmodesmata In a Lipid-dependent supporting

confidence: 73%

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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“…Lipid raft is a unique platform comprised by phospholipids, sterol and SLs that highly enriched in the PD-PM. Moreover, it was shown that PdBG2 protein, which attributes with lipid rafts at PD is mislocalized and induced callose deposition upon sterol depletion (Mongrand et al, 2004; Borner et al, 2005; Grison et al, 2015; Iswanto and Kim, 2017), and this subcellular localization alteration was also observed in the N. benthamiana leaves transiently expressing GFP:PdBG2 after Fen treatment ( Supplemental Fig. S3 ).…”

Section: Discussionmentioning

confidence: 88%

“…These intercellular channels play important roles in multicellular events during plant development by allowing the molecular exchange of signaling molecules such as transcription factors, RNAs, and growth regulators (Zambryski and Crawford, 2000; Maule, 2008; Wu et al, 2018). The plasmodesmal plasma membrane (PD-PM) is distinct from general cellular plasma membrane (PM) and is characterized by the enrichment of sterols and sphingolipid SL species (Grison et al, 2015; Iswanto and Kim, 2017; Mamode Cassim et al, 2019). The domains enriched with those special lipids are referred to as the membrane microdomain compartments, also called lipid rafts (Mongrand et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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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“…Recently, a possible cause for the differences in the behaviour and localization of PDLP1 and PDLP5 has been identified [82]. Pd-lining plasma membrane is known to contain specific regions in which sphingolipids interact with sterols to create specialized domains [106,108,109], where GPI-anchored proteins accumulate [39,56]. Moreover, sphingolipid biosynthesis is very important for modulating Pd function [110].…”

Section: Plasmodesmata-located Protein 5 (Pdlp5)mentioning

confidence: 99%

Plasmodesmata Conductivity Regulation: A Mechanistic Model

Dorokhov

Ershova

Sheshukova

et al. 2019

Plants

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Plant cells form a multicellular symplast via cytoplasmic bridges called plasmodesmata (Pd) and the endoplasmic reticulum (ER) that crosses almost all plant tissues. The Pd proteome is mainly represented by secreted Pd-associated proteins (PdAPs), the repertoire of which quickly adapts to environmental conditions and responds to biotic and abiotic stresses. Although the important role of Pd in stress-induced reactions is universally recognized, the mechanisms of Pd control are still not fully understood. The negative role of callose in Pd permeability has been convincingly confirmed experimentally, yet the roles of cytoskeletal elements and many PdAPs remain unclear. Here, we discuss the contribution of each protein component to Pd control. Based on known data, we offer mechanistic models of mature leaf Pd regulation in response to stressful effects.

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Lipid Raft, Regulator of Plasmodesmal Callose Homeostasis

Cited by 31 publications

References 85 publications

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

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

Plasmodesmata Conductivity Regulation: A Mechanistic Model

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