Localization of proteasomes in plant cells

Vallon, Ulrike; Kull, Ulrich

doi:10.1007/bf01403684

Cited by 10 publications

(7 citation statements)

References 34 publications

(11 reference statements)

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“…Putative NLS were also found in two Arabidopsis α‐type subunits Prc3_At and Prc1_At and in the β‐type subunit Prce_At (Table 1). Indications for both nuclear and cytoplasmic localization of proteasomes in plants have already been reported [49].…”

Section: Resultsmentioning

confidence: 92%

The 20S proteasome gene family in Arabidopsis thaliana

Parmentier¹,

Bouchez²,

Fleck³

et al. 1997

FEBS Letters

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The complexity of the proteasome gene family in higher plants was investigated by identification and sequencing cDNA clones from the Arabidopsis thaliana database showing homologies to 20S proteasome subunits. We identified plant counterparts for each of the 14 proteasomal subunit subfamilies. Moreover, several of them were highly related isoforms. Mapping data indicate a random distribution of the proteasome genes over the Arabidopsis genome.

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Section: Resultsmentioning

confidence: 92%

The 20S proteasome gene family in Arabidopsis thaliana

Parmentier¹,

Bouchez²,

Fleck³

et al. 1997

FEBS Letters

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“…Little data exist on the location of the proteosome in plants. They have been located in the cytoplasm of potato suspension cells by direct immunofluorescence, are possibly associated with elements of the cytoskeleton and may also reside in the nuclei (Vallon and Kull, 1994).…”

Section: Discussionmentioning

confidence: 99%

ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants

et al. 2003

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SummaryQuality control in the secretory pathway is a fundamental step in preventing deleterious effects that may arise by the release of malfolded proteins into the cell or apoplast. Our aims were to visualise and analyse the disposal route followed by aberrant proteins within a plant cell in vivo using fluorescent protein technology. A green fluorescent protein (GFP) fusion was detected in the cytosol and the nucleoplasm in spite of the presence of an N-terminal secretory signal peptide. In contrast to secreted GFP, the fusion protein was retained in the cells where it was degraded slowly, albeit at a rate much higher than that of the endoplasmic reticulum (ER)-retained derivative GFP-HDEL. The fusion protein could not be stabilised by inhibitors of transport or the cytosolic proteasome. However, the protein is a strong lumenal binding protein (BiP) ligand. Complete signal peptide processing even after long-term expression in virus-infected leaves rules out the possibility that the documented accumulation in the cytosol and nucleoplasm is because of the bypassing of the translocation pores. The data are consistent with the hypothesis that the fusion protein is disposed off from the ER via a retrograde translocation back to the cytosol. Moreover, accumulation in the nucleoplasm was shown to be microtubule dependent unlike the well-documented diffusion of cytosolically expressed GFP into the nucleoplasm. The apparent active transport of the GFP fusion into the nucleoplasm may indicate an as yet undiscovered feature of the ER-associated degradation (ERAD) pathway and explain the insensitivity to degradation by proteasome inhibitors.

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“…Gene-expression studies have documented the presence of ubiquitin and the proteasome in all plant parts, and within the cell this proteolytic system is observed in the nucleus as well as in the cytoplasm (Beers et al 1992; Vallon and Kull 1994;Ehlers et al 1996). Physiological as well as molecular studies have indicated a possible role for ubiquitin and the proteasome in proteolytic degradation during plant development (Genschik et al 1994;Umeda et al 1997;Bahrami and Gray 1999).…”

Section: Discussionmentioning

confidence: 94%

“…Ubiquitin and the proteasome are observed in the nucleus as well as in the cytoplasm (Beers et al 1992;Vallon and Kull 1994;Ehlers et al 1996). The intracellular localisation of the proteasome in yeast and mammal cell cultures as well as in plant protoplasts has been described in several reports, and the localisation of the proteasome is often found to be cell cycle dependent (Palmer et al 1994).…”

Section: Introductionmentioning

confidence: 95%

Immunohistochemical localisation of ubiquitin and the proteasome in sunflower ( Helianthus annuus cv. Giganteus)

Ingvardsen¹,

Veierskov²,

Joshi³

2001

Planta

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This study provides an immunohistochemical demonstration of the involvement of the ubiquitin- and proteasome-dependent pathway during differentiation and organogenesis in plants. The localisation of ubiquitin and the proteasome was studied in meristems, leaves, stems and roots of sunflower (Helianthus annuus L. cv. Giganteus). By using a new technique that enhances very low antigen signals, we obtained information on the structural distribution of the ubiquitin- and proteasome-dependent pathway, and of the importance of this pathway during organogenesis and plant development. Ubiquitin and the proteasome showed overall similarities in their cellular localisation. The highest antigenic signal was observed in the root and shoot apical meristems, in leaf primordia and vascular tissue. The cambium showed less expression than the apical meristems. During adventitious root formation in cuttings, no sign of increased expression was observed within dedifferentiating tissue, but as organogenesis progressed, the antigenic signal of ubiquitin and the proteasome gradually increased in the developing roots. Comparison of immunochemical results and Western blots demonstrated that important changes in the cellular antigen signal could only be detected by immunochemistry.

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Localization of proteasomes in plant cells

Cited by 10 publications

References 34 publications

The 20S proteasome gene family in Arabidopsis thaliana

The 20S proteasome gene family in Arabidopsis thaliana

ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants

Immunohistochemical localisation of ubiquitin and the proteasome in sunflower ( Helianthus annuus cv. Giganteus)

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