Separating Golgi Proteins from <i>Cis</i> to <i>Trans</i> Reveals Underlying Properties of Cisternal Localization

Parsons, Harriet T.; Stevens, Tim J.; McFarlane, Heather E.; Vidal‐Melgosa, Silvia; Griss, Johannes; Lawrence, Nicola; Butler, Richard J.; Sousa, Mirta Mittelstedt Leal de; Salemi, Michelle; Willats, William G. T.; Kim, Young-Mo; Heazlewood, Joshua L.; Lilley, Kathryn S.

doi:10.1105/tpc.19.00081

Cited by 45 publications

(49 citation statements)

References 102 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Analyses of the signal peptide (SP) and transmembrane (TM) span sequence properties were performed as previously described ( Parsons et al., 2019 ) with only minor modifications. SP-containing proteins and monotopic integral membrane proteins were identified using SignalP 4.1 ( Nielsen, 2017 ) and TMHMM 2.0 as described above.…”

Section: Methodsmentioning

confidence: 99%

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions

Barylyuk

Kořený

et al. 2020

Cell Host & Microbe

Self Cite

246

314

View full text Add to dashboard Cite

Summary Apicomplexan parasites cause major human disease and food insecurity. They owe their considerable success to highly specialized cell compartments and structures. These adaptations drive their recognition, nondestructive penetration, and elaborate reengineering of the host’s cells to promote their growth, dissemination, and the countering of host defenses. The evolution of unique apicomplexan cellular compartments is concomitant with vast proteomic novelty. Consequently, half of apicomplexan proteins are unique and uncharacterized. Here, we determine the steady-state subcellular location of thousands of proteins simultaneously within the globally prevalent apicomplexan parasite Toxoplasma gondii . This provides unprecedented comprehensive molecular definition of these unicellular eukaryotes and their specialized compartments, and these data reveal the spatial organizations of protein expression and function, adaptation to hosts, and the underlying evolutionary trajectories of these pathogens.

show abstract

Section: Methodsmentioning

confidence: 99%

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions

Barylyuk

Kořený

et al. 2020

Cell Host & Microbe

Self Cite

246

314

View full text Add to dashboard Cite

show abstract

“…The overlap with SYP32-mCherry was higher than that with SYP43-mCherry, indicating a slight enrichment in the cis- Golgi (Fig 2b and 2c). In further support of the Golgi localisation, both Arabidopsis GH43s were identified in Golgi-enriched cell extracts in global proteomics experiments (Parsons et al, 2012; Parsons et al, 2019).…”

Section: Resultsmentioning

confidence: 65%

Golgi-localized exo-β1,3-galactosidases involved in AGP modification and root cell expansion in Arabidopsis

Nibbering

Petersen

et al. 2020

Preprint

View full text Add to dashboard Cite

13 14 15 16 *corresponding author: Totte Niittylä, totte.niittyla@slu.se 17 18 19 20 48Plant arabinogalactan proteins (AGPs) are a diverse group of cell surface-and wall-associated 49 glycoproteins. Functionally important AGP glycans are synthesized in the Golgi apparatus, 50 but the relationships between their glycosylation, processing, and functionality are poorly 51 understood. Here we report the identification and functional characterization of two Golgi-52 localized exo-β-1,3-galactosidases from the glycosyl hydrolase 43 (GH43) family in 53 Arabidopsis thaliana. GH43 loss of function mutants exhibit root cell expansion defects in 54 sugar-containing growth media. This root phenotype is associated with an increase in the 55 extent of AGP cell wall association, as demonstrated by Yariv phenylglycoside dye 56 quantification and comprehensive microarray polymer profiling of sequentially extracted cell 57 walls. Recombinant GH43 characterization showed that the exo-β-1,3-galactosidase activity 58 of GH43s is hindered by β-1,6 branches on β-1,3-galactans. In line with this steric hindrance, 59 the recombinant GH43s did not release galactose from cell wall extracted glycoproteins or 60 AGP rich gum arabic. These results show that Arabidopsis GH43s are involved in AGP 61 glycan biosynthesis in the Golgi, and suggest their exo-β-1,3-galactosidase activity influences 62 AGP and cell wall matrix interactions, thereby adjusting cell wall extensibility. 63 64 65 66 67 68 69 70 71 72 73 74 75 76 77 78 et al. , 2010; Rose and Lee, 2010; Scheller and Ulvskov, 2010). The cell wall-associated 87 glycoproteins include arabinogalactan proteins (AGPs), which are proposed to have diverse 88 roles during cell expansion, including as structural components, modifiers of the extracellular 89 matrix, and ligands for cell surface receptors (Showalter et al., 2010; Xue et al., 2017). 90 91Glycans account for 90-98% of the molecular weight of AGPs, and are thought to be critical 92 for their functionality (Showalter, 1993). Characterisation of the enzymes responsible for 93 AGP glycosylation can elucidate AGP functions and functional redundancies (Showalter et 94 al., 2010; Showalter and Basu, 2016). AGP glycosylation is initiated by proline hydroxylation 95 in the ER and is then advanced in the Golgi apparatus by specialized glycosyl transferases 96 (GTs) (Rose and Lee, 2010; Hijazi et al., 2014). The glycosyl transferase family 31 (GT31) is 97 responsible for the synthesis of the hydroxyproline galactose and the β-1,3-galactan backbone 98

show abstract

“…While N-glycosylation begins in the endoplasmatic reticulum (ER) as co-translational en bloc transfer of a preformed oligosaccharide that is subsequently modified in the Golgi, type II AG biosynthesis is entirely Golgi-localized and depends on the hydroxylation of specific prolyl residues in the cis-Golgi followed by galactosylation of isolated Hyp residues and sequential build-up of type II AG in subsequent Golgi compartments. In a recent proteomics study, several P4H isoforms were found the cis and medial Golgi compartment, while HPGT2 was localized in the medial Golgi (Parsons et al, 2019). Some type II AG biosynthetic enzymes such as AtGALT31A have also been colocalized with exocyst protein Exo70E2 in a novel compartment, a finding whose significance remains to be investigated (Poulsen et al, 2014).…”

Section: Molecular Biology Of Type II Arabinogalactan Biosynthesismentioning

confidence: 97%

On the Potential Function of Type II Arabinogalactan O-Glycosylation in Regulating the Fate of Plant Secretory Proteins

Seifert

2020

Front. Plant Sci.

View full text Add to dashboard Cite

In a plant-specific mode of protein glycosylation, various sugars and glycans are attached to hydroxyproline giving rise to a variety of diverse O-glycoproteins. The sub-family of arabinogalactan proteins is implicated in a multitude of biological functions, however, the mechanistic role of O-glycosylation on AGPs by type II arabinogalactans is largely elusive. Some models suggest roles of the O-glycans such as in ligand-receptor interactions and as localized calcium ion store. Structurally different but possibly analogous types of protein O-glycosylation exist in animal and yeast models and roles for O-glycans were suggested in determining the fate of O-glycoproteins by affecting intracellular sorting or proteolytic activation and degradation. At present, only few examples exist that describe how the fate of artificial and endogenous arabinogalactan proteins is affected by O-glycosylation with type II arabinogalactans. In addition to other roles, these glycans might act as a molecular determinant for cellular localization and protein lifetime of many endogenous proteins.

show abstract

Separating Golgi Proteins from Cis to Trans Reveals Underlying Properties of Cisternal Localization

Cited by 45 publications

References 102 publications

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions

Golgi-localized exo-β1,3-galactosidases involved in AGP modification and root cell expansion in Arabidopsis

On the Potential Function of Type II Arabinogalactan O-Glycosylation in Regulating the Fate of Plant Secretory Proteins

Contact Info

Product

Resources

About