Sterols Modulate Cell-to-Cell Connectivity at Plasmodesmata

Farquharson, Kathleen L.

doi:10.1105/tpc.15.00218

Cited by 3 publications

(1 citation statement)

References 4 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As the loss of function of the α1-COP mutant showed enhanced PD callose phenotype, a question arises whether the subcellular localization of GPI-anchored proteins was perturbed in the α1-cop mutants. Previous studies have remarkably identified the effect of sterols along with SL alteration in the functions of GPI-anchored PD proteins, PdBG2 and PDCB1 (Farquharson, 2015; Grison et al, 2015; Iswanto and Kim, 2017; Iswanto et al, 2020). PdBGs belong to the group of GPI-anchored PD proteins, which are highly linked to sterol and SL-enriched lipid raft in planta .…”

Section: Resultsmentioning

confidence: 99%

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

Iswanto

Kumar

et al. 2021

Preprint

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

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

Iswanto

Kumar

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

Bibliography

2019

Plant Cell Biology

View full text Add to dashboard Cite

α1‐COP modulates plasmodesmata function through sphingolipid enzyme regulation

Iswanto,

Vu,

Shon

et al. 2024

JIPB

View full text Add to dashboard Cite

Callose, a β‐1,3‐glucan plant cell wall polymer, regulates symplasmic channel size at plasmodesmata (PD) and plays a crucial role in a variety of plant processes. However, elucidating the molecular mechanism of PD callose homeostasis is limited. We screened and identified an Arabidopsis mutant plant with excessive callose deposition at PD and found that the mutated gene was α1‐COP, a member of the coat protein I (COPI) coatomer complex. We report that loss of function of α1‐COP elevates the callose accumulation at PD by affecting subcellular protein localization of callose degradation enzyme PdBG2. This process is linked to the functions of ERH1, an inositol phosphoryl ceramide synthase, and glucosylceramide synthase through physical interactions with the α1‐COP protein. Additionally, the loss of function of α1‐COP alters the subcellular localization of ERH1 and GCS proteins, resulting in a reduction of GlcCers and GlcHCers molecules, which are key sphingolipid (SL) species for lipid raft formation. Our findings suggest that α1‐COP protein, together with SL modifiers controlling lipid raft compositions, regulates the subcellular localization of GPI‐anchored PDBG2 proteins, and hence the callose turnover at PD and symplasmic 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.

show abstract

Sterols Modulate Cell-to-Cell Connectivity at Plasmodesmata

Cited by 3 publications

References 4 publications

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

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

Bibliography

α1‐COP modulates plasmodesmata function through sphingolipid enzyme regulation

Contact Info

Product

Resources

About