The Ultrastructure and Computer-enhanced Digital Image Analysis of Plasmodesmata at the Kranz Mesophyll-Bundle Sheath Interface of Themeda triandra var. imberbis (Retz) A. Camus in Conventionally-fixed Blades

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

doi:10.1006/anbo.1993.1106

Cited by 69 publications

(43 citation statements)

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“…Potential mechanisms involving the modification of two plasmodesmal regions, the cytoplasmic sleeve and the neck, during active gating are illustrated in Figure 2. As shown in Figure 28, Botha et al, 1993;Evert et al, 1996), may be an artifact of sample preparation. Figure 2 6 also shows an extracellular sphincter, which has been proposed to modulate neck permeability and structure (Overall and Blackman, 1996).…”

Section: Models For Plasmodesmal Architecture During Gatingmentioning

confidence: 99%

“…Models mostly depict plasmodesmal channels as a linear tubular arrangement of microchannels traversing the cell wall. However, direct observation as well as computer-generated models suggest that microchannels are spirally arranged (Ding et ai., 1992;Botha et al, 1993;Badelt et al, 1994;Overall and Blackman, 1996). Such a spiral arrangement may simplify the mechanics of moving macromolecules.…”

Section: Models For Plasmodesmal Architecture During Gatingmentioning

confidence: 99%

See 1 more Smart Citation

Plant intercellular communication via plasmodesmata.

McLean¹,

Hempel²,

Zambryski³

1997

Plant Cell

168

103

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Section: Models For Plasmodesmal Architecture During Gatingmentioning

confidence: 99%

Section: Models For Plasmodesmal Architecture During Gatingmentioning

confidence: 99%

Plant intercellular communication via plasmodesmata.

McLean¹,

Hempel²,

Zambryski³

1997

Plant Cell

168

103

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“…Between the concentric membranes is a sleeve that interconnects the cytoplasm of the neighboring cells. Highresolution electron micrographs reveal that within this sleeve are particles that have been variously interpreted as being embedded in the PM (Ding et al, 1992) and/or in the desmotubule (Botha et al, 1993) or to be present entirely within the cytoplasmic sleeve (Overall, 1999).…”

Section: Introductionmentioning

confidence: 99%

Class 1 Reversibly Glycosylated Polypeptides Are Plasmodesmal-Associated Proteins Delivered to Plasmodesmata via the Golgi Apparatus

et al. 2005

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SE-WAP41, a salt-extractable 41-kD wall-associated protein that is associated with walls of etiolated maize (Zea mays) seedlings and is recognized by an antiserum previously reported to label plasmodesmata and the Golgi, was cloned, sequenced, and found to be a class 1 reversibly glycosylated polypeptide (C1RGP). Protein gel blot analysis of cell fractions with an antiserum against recombinant SE-WAP41 showed it to be enriched in the wall fraction. RNA gel blot analysis along the mesocotyl developmental axis and during deetiolation demonstrates that high SE-WAP41 transcript levels correlate spatially and temporally with primary and secondary plasmodesmata (Pd) formation. All four of the Arabidopsis thaliana C1RGP proteins, when fused to green fluorescent protein (GFP) and transiently expressed in tobacco (Nicotiana tabacum) epidermal cells, display fluorescence patterns indicating they are Golgi- and plasmodesmal-associated proteins. Localization to the Golgi apparatus was verified by colocalization of transiently expressed AtRGP2 fused to cyan fluorescence protein together with a known Golgi marker, Golgi Nucleotide Sugar Transporter 1 fused to yellow fluorescent protein (GONST1:YFP). In transgenic tobacco, AtRGP2:GFP fluorescence is punctate, is present only in contact walls between cells, and colocalizes with aniline blue–stained callose present around Pd. In plasmolyzed cells, AtRGP2:GFP remains wall embedded, whereas GONST1:YFP cannot be found embedded in cell walls. This result implies that the targeting to Pd is not due to a default pathway for Golgi-localized fusion proteins but is specific to C1RGPs. Treatment with the Golgi disrupting drug Brefeldin A inhibits Pd labeling by AtRGP2:GFP. Integrating these data, we conclude that C1RGPs are plasmodesmal-associated proteins delivered to plasmodesmata via the Golgi apparatus.

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“…These central rod particles, along with the proteins embedded in the outer membrane of the desmotubule cylinder, are believed to occlude the desmotubule lumen . However, this may be due to the fixation protocol employed, since other workers have estimated that the space between the central particles is between 2.5 and 3 nm (Botha et al 1993).…”

Section: The Er Lumenmentioning

confidence: 98%

“…On the basis of ultrastructure alone, plasmodesmata are classified into two basic types: simple and branched. The majority of models describe the structure of simple plasmodesmata, and interpretations have been influenced by the effects of the various fixation and staining procedures on plasmodesmata (Gunning and Robards 1976;Robards and Lucas 1990;Beebe and Turgeon 1991;Tilney et al 1991;Ding et al 1992b;Botha et al 1993;Turner et al 1994;White et al 1994;Overall and Blackman 1996;Ding 1997Ding , 1999Waigmann et al 1997;Overall 1999). Although there is consensus that all plasmodesmata have the same basic configuration, there is still much debate about their fine structure.…”

Section: Structurementioning

confidence: 99%

The ER Within Plasmodesmata

Wright¹,

Oparka²

2006

Plant Cell Monographs

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The endoplasmic reticulum (ER) is an essential component of plasmodesmata, the membrane-lined pores that interconnect plant cells. The desmotubule which traverses the centre of a plasmodesma is formed from, and continuous with, the cortical ER. Whilst the exact role of the ER is only now being characterised, it is recognised that the ER is intimately involved in the transfer of molecules to and through plasmodesmata, providing a number of pathways for movement between cells as well as being implicated in the mechanisms that control transport. It is believed that molecules may be transported by passive flow within the desmotubule lumen, by diffusion along the inner desmotubule membranes or by specific attachment to the cytoplasmic face of the desmotubule followed by facilitated transport through the cytoplasmic sleeve. The ER is also involved in the formation of plasmodesmata either during cell division or when formed de novo across non-division walls. This chapter focusses on the role of the ER in plasmodesmatal formation and function.

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The Ultrastructure and Computer-enhanced Digital Image Analysis of Plasmodesmata at the Kranz Mesophyll-Bundle Sheath Interface of Themeda triandra var. imberbis (Retz) A. Camus in Conventionally-fixed Blades

Cited by 69 publications

References 0 publications

Plant intercellular communication via plasmodesmata.

Plant intercellular communication via plasmodesmata.

Class 1 Reversibly Glycosylated Polypeptides Are Plasmodesmal-Associated Proteins Delivered to Plasmodesmata via the Golgi Apparatus

The ER Within Plasmodesmata

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