The Rate of Phaseolin Assembly Is Controlled by the Glucosylation State of Its N-Linked Oligosaccharide Chains

Lupattelli, Francesca; Bollini, Roberto; Vitale, Alessandro; Ceriotti, Aldo

doi:10.2307/3870510

Cited by 16 publications

(6 citation statements)

References 35 publications

(61 reference statements)

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“…However, circumstantial evidence supports the idea that the calnexin ⁄ calreticulin cycle is present in plant cells [132]. For example, it has been shown in in vitro translation systems with wheat germ extract and bean microsomes that the rate of phaseolin assembly is accelerated when a glucosidase inhibitor is included to stop glucose trimming of the N-glycan [133]. In this system, phaseolin with partially trimmed glycans was unable to assemble into trimers, probably because of being trapped by calnexin or calreticulin.…”

Section: Foldingmentioning

confidence: 97%

Cellular response to unfolded proteins in the endoplasmic reticulum of plants

2007

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Secretory and transmembrane proteins are synthesized in the endoplasmic reticulum (ER) in eukaryotic cells. Nascent polypeptide chains, which are translated on the rough ER, are translocated to the ER lumen and folded into their native conformation. When protein folding is inhibited because of mutations or unbalanced ratios of subunits of hetero‐oligomeric proteins, unfolded or misfolded proteins accumulate in the ER in an event called ER stress. As ER stress often disturbs normal cellular functions, signal‐transduction pathways are activated in an attempt to maintain the homeostasis of the ER. These pathways are collectively referred to as the unfolded protein response (UPR). There have been great advances in our understanding of the molecular mechanisms underlying the UPR in yeast and mammals over the past two decades. In plants, a UPR analogous to those in yeast and mammals has been recognized and has recently attracted considerable attention. This review will summarize recent advances in the plant UPR and highlight the remaining questions that have yet to be addressed.

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Section: Foldingmentioning

confidence: 97%

Cellular response to unfolded proteins in the endoplasmic reticulum of plants

2007

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“…The membrane bound calnexin (CNX) and its soluble luminal homolog calreticulin (CRT) are chaperones that facilitate maturation and detection of defective folding (Lederkremer, 2009). The cleavage of the terminal glucose residues of the N -glycans can be crucial to protein folding (Lupattelli et al, 1997). Indeed, the mono-glycosylated core glycan (Figure 1, GlcMan9GlcNAc2) generates the interaction with the CNX/CRT complex (Ruddock and Molinari, 2006).…”

Section: Biosynthesis Of N-glycoproteinsmentioning

confidence: 99%

The Secreted Plant N-Glycoproteome and Associated Secretory Pathways

Ruiz‐May¹,

Kim²,

Brandizzí³

et al. 2012

Front. Plant Sci.

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N-Glycosylation is a common form of eukaryotic protein post-translational modification, and one that is particularly prevalent in plant cell wall proteins. Large scale and detailed characterization of N-glycoproteins therefore has considerable potential in better understanding the composition and functions of the cell wall proteome, as well as those proteins that reside in other compartments of the secretory pathway. While there have been numerous studies of mammalian and yeast N-glycoproteins, less is known about the population complexity, biosynthesis, structural variation, and trafficking of their plant counterparts. However, technical developments in the analysis of glycoproteins and the structures the glycans that they bear, as well as valuable comparative analyses with non-plant systems, are providing new insights into features that are common among eukaryotes and those that are specific to plants, some of which may reflect the unique nature of the plant cell wall. In this review we present an overview of the current knowledge of plant N-glycoprotein synthesis and trafficking, with particular reference to those that are cell wall localized.

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“…The a-amylase overexpression plasmid (pNL200; Leborgne-Castel et al, 1999) was co-transfected with an empty expression vector (pDHA) or vectors encoding either of the following constructs: BiP (Leborgne-Castel et al, 1999), endoplasmin (this paper), secreted GFP (mGFP5; Frigerio et al, 2001a) or T343F phaseolin (T343F; Lupattelli et al, 1997). The effects of the non-glycosylated, secreted mGFP5 and the glycosylated, vacuolar protein T343F were investigated as further negative controls, besides the empty vector, because the two proteins are introduced into the ER but should not possess chaperone activity.…”

Section: Under Tm Stress Endoplasmin Supports Secretory Protein Synthmentioning

confidence: 99%

Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues

et al. 2006

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SummaryEndoplasmin is a molecular chaperone of the heat-shock protein 90 class located in the endoplasmic reticulum and its activity is poorly characterized in plants. We assessed the ability of endoplasmin to alleviate stress via its transient overexpression in tobacco protoplasts treated with tunicamycin, an inhibitor of glycosylation and inducer of the unfolded protein response (UPR). Endoplasmin supported the secretion of a model secretory protein but was less effective than BiP, the endoplasmic reticulum member of the heat-shock protein 70 family. Consistently, immunoprecipitation experiments with in vivo radioactively labelled proteins using an antiserum prepared against Arabidopsis endoplasmin showed that a much smaller number of newly synthesized polypeptides associated with endoplasmin than with BiP. Synthesis of endoplasmin was enhanced by UPR inducers in tobacco seedlings but not protoplasts. As BiP synthesis was induced in both systems, we conclude that the UPR acts differently, at least in part, on the expression of the two chaperones. Endoplasmin was not detectable in extracts of leaves and stems of the Arabidopsis endoplasmin T-DNA insertion mutant shepherd. However, the chaperone is present, albeit at low levels, in shepherd mutant callus, mature roots and tunicamycin-treated seedlings, demonstrating that the mutation is leaky. Reduced endoplasmin in the shepherd mutant has no effect on BiP protein levels in callus or mature roots, leaves and stems, but is compensated by increased BiP in seedlings. This increase occurs in proliferating rather than expanding leaf cells, indicating an important role for endoplasmin in proliferating plant tissues.

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The Rate of Phaseolin Assembly Is Controlled by the Glucosylation State of Its N-Linked Oligosaccharide Chains

Cited by 16 publications

References 35 publications

Cellular response to unfolded proteins in the endoplasmic reticulum of plants

Cellular response to unfolded proteins in the endoplasmic reticulum of plants

The Secreted Plant N-Glycoproteome and Associated Secretory Pathways

Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues

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