Biology Publications
Document Type
Article
Publication Date
1-16-2023
Journal
Plant Signaling & Behavior
Volume
18
Issue
1
URL with Digital Object Identifier
https://doi.org/10.1080/15592324.2022.2164670
Abstract
Cell-to-cell communication via membranous channels called plasmodesmata (PD) plays critical rolesduring plant development and in response to biotic and abiotic stresses. Several enzymes and receptor-like proteins (RLPs), including Arabidopsis thaliana glucan synthase-likes (GSLs), also known as callosesynthases (CALSs), and PD-located proteins (PDLPs), have been implicated in plasmodesmal permeabilityregulation and intercellular communication. Localization of PDLPs to punctate structures at the cellperiphery and their receptor-like identity have raised the hypothesis that PDLPs are involved in theregulation of symplastic trafficking during plant development and in response to endogenous andexogenous signals. Indeed, it was shown that PDLP5 could limit plasmodesmal permeability throughinducing an increase in callose accumulation at PD. However, mechanistically, how this is achievedremains to be elucidated. To address this key issue in understanding the regulation of PD, physical andfunctional interactions between PDLPs and GSLs (using the PDLP5–GSL8/CALS10 pair as a model) wereinvestigated. Our results show that GSL8/CALS10 plays essential roles and is required for the function andplasmodesmal localization of PDLP5. Furthermore, it was demonstrated that the localization of PDLP5 toPD and its function in inducing callose deposition are GSL8-dependent. Importantly, our transgenic studyshows that three key members of the GSL family, i.e., GSL5/CALS12, GSL8/CALS10, and GSL12/CALS3,localize to PD and co-localize with PDLP5, suggesting that GSL8/CALS10 might not be the only callosesynthase with the determining role in PD regulation. These findings, together with our previous observa-tion showing the direct interaction of GSL8/CALS10 with PDLP5, indicate the pivotal role of the GSL8/CALS10-PDLP5 interplay in regulating PD permeability. Future work is needed to investigate whether thePDLP5 functionality and localization are also disrupted in gsl5 and gsl12, or it is just gsl8-specific.
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