α1-COP modulates plasmodesmata function through sphingolipid enzyme regulation

Arya Bagus Boedi Iswanto, Minh Huy Vu, Jong Cheol Shon, Ritesh Kumar, Shuwei Wu, Hobin Kang, Da Ran Kim, Geon Hui Son, Woe Yoen Kim, Youn Sig Kwak, Kwang Hyeon Liu, Sang Hee Kim, Jae Yean Kim

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)1639-1657
Number of pages19
JournalJournal of Integrative Plant Biology
Volume66
Issue number8
DOIs
StatePublished - Aug 2024

Keywords

  • callose
  • coatomer proteins
  • membrane-bound vesicle
  • plasmodesmata
  • sphingolipid enzymes

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