Towards reconciliation of structure with function in plasmodesmata—who is the gatekeeper?

Botha, C. E. J.; Cross, R. H. M.

doi:10.1016/s0968-4328(99)00108-0

Cited by 46 publications

(20 citation statements)

References 26 publications

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“…Our data on the co-localization of callose deposits and TGBp3-induced bodies strongly support this hypothesis ( Fig. 6F-H) (see Botha & Cross, 2000;Blackman & Overall, 2001;Cowan et al, 2002). Fluorescent microscopy of N. benthamiana expressing GFP-18K revealed that the peripheral bodies are pulled away from the plant cell wall together with the plasma membrane during mannitolinduced plasmolysis (Fig.…”

Section: Discussionsupporting

confidence: 75%

Immunodetection and fluorescent microscopy of transgenically expressed hordeivirus TGBp3 movement protein reveals its association with endoplasmic reticulum elements in close proximity to plasmodesmata

Gorshkova

Erokhina

Строганова

et al. 2003

Journal of General Virology

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The subcellular localization of the hydrophobic TGBp3 protein of Poa semilatent virus (PSLV, genus Hordeivirus) was studied in transgenic plants using fluorescent microscopy to detect green fluorescent protein (GFP)-tagged protein and immunodetection with monoclonal antibodies (mAbs) raised against the GFP-based fusion expressed in E. coli. In Western blot analysis, mAbs efficiently recognized the wild-type and GFP-fused PSLV TGBp3 proteins expressed in transgenic Nicotiana benthamiana, but failed to detect TGBp3 in hordeivirus-infected plants. It was found that PSLV TGBp3 and GFP-TGBp3 had a tendency to form large protein complexes of an unknown nature. Fractionation studies revealed that TGBp3 represented an integral membrane protein and probably co-localized with an endoplasmic reticulum-derived domain. Microscopy of epidermal cells in transgenic plants demonstrated that GFP-TGBp3 localized to cell wall-associated punctate bodies, which often formed pairs of opposing discrete structures that co-localized with callose, indicating their association with the plasmodesmata-enriched cell wall fields. After mannitol-induced plasmolysis of the leaf epidermal cells in the transgenic plants, TGBp3 appeared within the cytoplasm and not at cell walls. Although TGBp3-induced bodies were normally static, most of them became motile after plasmolysis and displayed stochastic motion in the cytoplasm.

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Section: Discussionsupporting

confidence: 75%

Immunodetection and fluorescent microscopy of transgenically expressed hordeivirus TGBp3 movement protein reveals its association with endoplasmic reticulum elements in close proximity to plasmodesmata

Gorshkova

Erokhina

Строганова

et al. 2003

Journal of General Virology

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“…In land plants, there have been many reports of plasmodesmatal internal components at the ultrastructural level (Ding et al 1992b, Botha andCross 2000), i.e. a desmotubule passing through the entire canal (Robards and Lucas 1990), particular structures on the inner plasma membrane and on the outer membrane of the desmotubule, and spoke-like extensions.…”

Section: Ultrastructure Of Plasmodesmata In Brown Algaementioning

confidence: 99%

Ultrastructural study of plasmodesmata in the brown alga Dictyota dichotoma (Dictyotales, Phaeophyceae)

Terauchi

Nagasato

Kajimura

et al. 2012

Planta

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“…Callose deposition at Pds is stimulated by physical and physiological stresses (Hughes and Gunning, 1980;Beffa and Meins, 1996;Iglesias and Meins, 2000;Sivaguru et al, 2000;Rinne et al, 2005;Ueki and Citovsky, 2005;Maeda et al, 2006) and is proposed to provide a mechanism for regulating Pd flux (Botha and Cross, 2000;Iglesias and Meins, 2000;Levy et al, 2007a). Hence, for example, plants with reduced accumulation of the glycolytic enzyme 1,3-b-glucanase had increased callose accumulation and a reduction in the experimental molecular size exclusion limit.…”

Section: Introductionmentioning

confidence: 99%

AnArabidopsisGPI-Anchor Plasmodesmal Neck Protein with Callose Binding Activity and Potential to Regulate Cell-to-Cell Trafficking

et al. 2009

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Plasmodesmata (Pds) traverse the cell wall to establish a symplastic continuum through most of the plant. Rapid and reversible deposition of callose in the cell wall surrounding the Pd apertures is proposed to provide a regulatory process through physical constriction of the symplastic channel. We identified members within a larger family of X8 domaincontaining proteins that targeted to Pds. This subgroup of proteins contains signal sequences for a glycosylphosphatidylinositol linkage to the extracellular face of the plasma membrane. We focused our attention on three closely related members of this family, two of which specifically bind to 1,3-b-glucans (callose) in vitro. We named this family of proteins Pd callose binding proteins (PDCBs). Yellow fluorescent protein-PDCB1 was found to localize to the neck region of Pds with potential to provide a structural anchor between the plasma membrane component of Pds and the cell wall. PDCB1, PDCB2, and PDCB3 had overlapping and widespread patterns of expression, but neither single nor combined insertional mutants for PDCB2 and PDCB3 showed any visible phenotype. However, increased expression of PDCB1 led to an increase in callose accumulation and a reduction of green fluorescent protein (GFP) movement in a GFP diffusion assay, identifying a potential association between PDCB-mediated callose deposition and plant cell-to-cell communication.

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Towards reconciliation of structure with function in plasmodesmata—who is the gatekeeper?

Cited by 46 publications

References 26 publications

Immunodetection and fluorescent microscopy of transgenically expressed hordeivirus TGBp3 movement protein reveals its association with endoplasmic reticulum elements in close proximity to plasmodesmata

Immunodetection and fluorescent microscopy of transgenically expressed hordeivirus TGBp3 movement protein reveals its association with endoplasmic reticulum elements in close proximity to plasmodesmata

Ultrastructural study of plasmodesmata in the brown alga Dictyota dichotoma (Dictyotales, Phaeophyceae)

AnArabidopsisGPI-Anchor Plasmodesmal Neck Protein with Callose Binding Activity and Potential to Regulate Cell-to-Cell Trafficking

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