Arabinogalactan biosynthesis: Implication of AtGALT29A enzyme activity regulated by phosphorylation and co-localized enzymes for nucleotide sugar metabolism in the compartments outside of the Golgi apparatus

Poulsen, Carsten Stig; Dilokpimol, Adiphol; Geshi, Naomi

doi:10.4161/15592324.2014.984524

Cited by 15 publications

(8 citation statements)

References 20 publications

(25 reference statements)

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“…For example, many GAPs in plants contain N ‐ and/or O ‐linked glycans that could reinforce transport to the outer leaflet of the PM due to protein‐carbohydrate and/or carbohydrate‐carbohydrate interactions within microdomains. Glycosyltransferases (GTs) involved in O ‐glycosylation have also been identified in exocyst‐positive organelles (EXPOs) that are part of the unconventional protein secretion pathway (Poulsen et al ; Poulsen et al ). This has led to the experimentally unverified suggestion that GPI‐AGPs could be secreted via the EXPO pathway to direct targeted or polarized secretion (van de Meene et al ).…”

Section: Delivery Of Gaps To the Cell Surface − Association With Lipimentioning

confidence: 99%

“…Glycosyltransferases (GTs) involved in O-glycosylation have also been identified in exocyst-positive organelles (EXPOs) that are part of the unconventional protein secretion pathway (Poulsen et al 2014;Poulsen et al 2015). This has led to the experimentally unverified suggestion that GPI-AGPs could be secreted via the EXPO pathway to direct targeted or polarized secretion (van de Meene et al 2017).…”

Section: Biosynthesis Of Gpi-anchored Proteins In Plantsmentioning

confidence: 99%

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Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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Approximately 1% of plant proteins are predicted to be post-translationally modified with a glycosylphosphatidylinositol (GPI) anchor that tethers the polypeptide to the outer leaflet of the plasma membrane. Whereas the synthesis and structure of GPI anchors is largely conserved across eukaryotes, the repertoire of functional domains present in the GPI-anchored proteome has diverged substantially. In plants, this includes a large fraction of the GPI-anchored proteome being further modified with plant-specific arabinogalactan (AG) O-glycans. The importance of the GPI-anchored proteome to plant development is underscored by the fact that GPI biosynthetic null mutants exhibit embryo lethality. Mutations in genes encoding specific GPI-anchored proteins (GAPs) further supports their contribution to diverse biological processes, occurring at the interface of the plasma membrane and cell wall, including signaling, cell wall metabolism, cell wall polymer cross-linking, and plasmodesmatal transport. Here, we review the literature concerning plant GPI-anchored proteins, in the context of their potential to act as molecular hubs that mediate interactions between the plasma membrane and the cell wall, and their potential to transduce the signal into the protoplast and, thereby, activate signal transduction pathways.

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Section: Delivery Of Gaps To the Cell Surface − Association With Lipimentioning

confidence: 99%

Section: Biosynthesis Of Gpi-anchored Proteins In Plantsmentioning

confidence: 99%

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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“…These proposed pathways are consistent with experimental data demonstrating that some cell wall-related proteins follow a UPS mechanism probably involving EV derived from MVB or EXPO ( Davis et al , 2016 ). This is the case for an arabinogalactan glycosyltransferase ( Poulsen et al , 2014 ), the S -adenosylmethionine synthase 2 ( Wang et al , 2010 ) and the UDP-glucuronate epimerases 1 and 6 ( Poulsen et al , 2015 ). Our results suggest that these examples may not be exceptional cases but rather the first among a large number of cell wall proteins secreted using an EV-dependent mechanism.…”

Section: Cell Wall-related Proteins In Sunflower Evmentioning

confidence: 99%

Extracellular vesicles: a missing component in plant cell wall remodeling

Canal

Pinedo

2018

Journal of Experimental Botany

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“…The DUF576 family methyltransferases that act against AGP glycan have been detected not only in the Golgi apparatus but also in small punctate structures that are distinct from the Golgi apparatus (Temple et al, 2019). Similarly, a subset of glycosyltransferases involved in AGP glycan biogenesis was found in a non-Golgi punctate structure with an exocyst protein Exo70 homolog 2, which is a marker for exocyst-positive organelles, but not with a SNARE protein SYP61, which is localized in the trans-Golgi network (TGN) and subsequent secretory vesicles (Poulsen et al, 2015). Recent analysis of the secretome of Arabidopsis indicated that there are at least two distinct secretory pathways in Arabidopsis leaf cells (Uemura et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

Glycosylphosphatidylinositol-anchoring is required for the proper transport and glycosylation of classical arabinogalactan protein precursor in tobacco BY-2 cells

Nagasato

Sugita

Tsuno

et al. 2020

Preprint

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Arabinogalactan proteins (AGPs) are extracellular proteoglycans with many O-linked glycan chains. Precursors to many AGPs contain a C-terminal signal for the addition of a GPI-anchor, yet the role of this modification has not been elucidated. NtAGP1, a tobacco precursor to AGP, comprises a signal peptide, an AGP-coding region and a GPI-anchoring signal, and classified as a member of classical AGP. Using green fluorescent protein (GFP) and sweet potato sporamin (SPO) as tags and tobacco BY-2 cells as the host, we analyzed the transport and modification of NtAGP1. The fusion protein of GFP or SPO and NtAGP1 expressed in BY-2 cells migrated as a large smear on SDS-polyacrylamide gel. Confocal microscopic analysis indicated that the GFP and NtAGP1 fusion protein localized to the plasma membrane (PM), and fractionation studies of microsomes indicated that the majority of the fusion protein of SPO and NtAGP1 (SPO-AGP) localized to the PM. In contrast, the expression of mutants without a GPI-anchoring signal yielded several forms, and the largest forms migrating as large smears on the gel were secreted into the culture medium, whereas other forms were recovered in the endomembrane organelles. Comparison of the glycan structures of the SPO-AGP recovered in microsomes and the secreted mutant SPO-AGP without a GPI-anchoring signal using antibodies against AGP glycan epitopes indicated that the glycan structures of these proteins are different. These observations indicated that a GPI-anchoring signal is required for both the proper transport and glycosylation of the AGP precursor.

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Arabinogalactan biosynthesis: Implication of AtGALT29A enzyme activity regulated by phosphorylation and co-localized enzymes for nucleotide sugar metabolism in the compartments outside of the Golgi apparatus

Cited by 15 publications

References 20 publications

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Extracellular vesicles: a missing component in plant cell wall remodeling

Glycosylphosphatidylinositol-anchoring is required for the proper transport and glycosylation of classical arabinogalactan protein precursor in tobacco BY-2 cells

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