Actin associated with plasmodesmata

White, Rosemary G.; Badelt, K.; Overall, Robyn L.; Vesk, Maret

doi:10.1007/bf01507853

Cited by 208 publications

(140 citation statements)

References 62 publications

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“…It is well established that the cortical ER system is dynamic (Allen and Brown, 1988;Hepler et al, 1990;Grabski, 1993;Cantrill et al, 1999), and actin has been implicated in cortical ER movements (Quader et al, 1987) as well as in providing a "scaffold" for trafficking ER-associated Golgi stacks (Boevink et al, 1996). Inhibitors of the actin cytoskeleton increase the size exclusion limit of plasmodesmata (Ding, 1996), and actin and myosin have been immunolocalized to plasmodesmata (White et al, 1994;Radford and White, 1998;Baluska et al, 2000). Therefore, we suggest that future studies address the role of actin as a potential cytoskeletal element for transporting ER-bound vRNA complexes to, and through, higher plant plasmodesmata.…”

Section: Discussionmentioning

confidence: 99%

Functional Analysis of a DNA-Shuffled Movement Protein Reveals That Microtubules Are Dispensable for the Cell-to-Cell Movement of Tobacco mosaic virus

Gillespie¹,

Boevink²,

Haupt³

et al. 2002

Plant Cell

162

171

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Section: Discussionmentioning

confidence: 99%

Functional Analysis of a DNA-Shuffled Movement Protein Reveals That Microtubules Are Dispensable for the Cell-to-Cell Movement of Tobacco mosaic virus

Gillespie¹,

Boevink²,

Haupt³

et al. 2002

Plant Cell

162

171

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“…Ultrastructural studies of plant cells have revealed the close association of ER tubules and actin bundles within the cortical cytoplasm (Goosen-de Roo et al, 1983;Lichtscheidl et al, 1990;White et al, 1994), and video microscopy of cytoplasmic streaming has shown sliding of the ER network along stationary actin cables in lower-plant characean algae cells (Kachar and Reese, 1988). Even though most cortical ER tubules do not co-align with cortical actin filaments in yeast, the disruption of actin assembly results in a rapid and dramatic decrease in cortical ER dynamics (Prinz et al, 2000).…”

Section: Actin and Myosin V In Er Movementmentioning

confidence: 99%

Dynamics and inheritance of the endoplasmic reticulum

Ferro‐Novick

Novick³

2004

Journal of Cell Science

134

124

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The endoplasmic reticulum (ER) consists of a polygonal array of interconnected tubules and sheets that spreads throughout the eukaryotic cell and is contiguous with the nuclear envelope. This elaborate structure is created and maintained by a constant remodeling process that involves the formation of new tubules, their cytoskeletal transport and homotypic fusion. Since the ER is a large, single-copy organelle, it must be actively segregated into daughter cells during cell division. Recent analysis in budding yeast indicates that ER inheritance involves the polarized transport of cytoplasmic ER tubules into newly formed buds along actin cables by a type V myosin. The tubules then become anchored to a site at the bud tip and this requires the Sec3p subunit of the exocyst complex. The ER is then propagated along the cortex of the bud to yield a cortical ER structure similar to that of the mother cell. In animal cells, the ER moves predominantly along microtubules, whereas actin fibers serve a complementary role. It is not yet clear to what extent the other components controlling ER distribution in yeast might be conserved in animal cells.

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“…A number of proteins affect the structure and functional performance of the PD, which in turn impacts the cell-to-cell transport of small and large molecules through the PD during plant growth, development, and defense (Cilia and Jackson, 2004;Sagi et al, 2005;Lucas et al, 2009;Simpson et al, 2009;Stonebloom et al, 2009). For example, actin and myosin, which link the desmotubule to the plasma membrane (PM) at the neck region of PD, are believed to play a role in regulating PD permeability by controlling PD aperture (White et al, 1994;Ding et al, 1996;Reichelt et al, 1999). Callose deposition can also impact the size of the PD aperture at the neck region (Radford et al, 1998;Levy et al, 2007) and callose synthase genes such as Glucan SynthaseLike7 (GSL7, also named CalS7), GSL8, and GSL12 have been shown to play a role in regulating symplastic trafficking (Guseman et al, 2010;Barratt et al, 2011;Vatén et al, 2011;Xie et al, 2011).…”

mentioning

confidence: 99%

Grain setting defect1, Encoding a Remorin Protein, Affects the Grain Setting in Rice through Regulating Plasmodesmatal Conductance

et al. 2014

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Effective grain filling is one of the key determinants of grain setting in rice (Oryza sativa). Grain setting defect1 (GSD1), which encodes a putative remorin protein, was found to affect grain setting in rice. Investigation of the phenotype of a transfer DNA insertion mutant (gsd1-Dominant) with enhanced GSD1 expression revealed abnormalities including a reduced grain setting rate, accumulation of carbohydrates in leaves, and lower soluble sugar content in the phloem exudates. GSD1 was found to be specifically expressed in the plasma membrane and plasmodesmata (PD) of phloem companion cells. Experimental evidence suggests that the phenotype of the gsd1-Dominant mutant is caused by defects in the grain-filling process as a result of the impaired transport of carbohydrates from the photosynthetic site to the phloem. GSD1 functioned in affecting PD conductance by interacting with rice ACTIN1 in association with the PD callose binding protein1. Together, our results suggest that GSD1 may play a role in regulating photoassimilate translocation through the symplastic pathway to impact grain setting in rice.

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Actin associated with plasmodesmata

Cited by 208 publications

References 62 publications

Functional Analysis of a DNA-Shuffled Movement Protein Reveals That Microtubules Are Dispensable for the Cell-to-Cell Movement of Tobacco mosaic virus

Functional Analysis of a DNA-Shuffled Movement Protein Reveals That Microtubules Are Dispensable for the Cell-to-Cell Movement of Tobacco mosaic virus

Dynamics and inheritance of the endoplasmic reticulum

Grain setting defect1, Encoding a Remorin Protein, Affects the Grain Setting in Rice through Regulating Plasmodesmatal Conductance

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