ArticlePlant physiology2012
Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers, 1 of them a synthesis that pooled it.
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Who cites it
89 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.
- Assessing sub-cellular resolution in spatial proteomics experiments.Current opinion in chemical biology · 2019Pooled it
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- NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ion Changes and Signaling under Salt Stress in Wheat and Other Important Crops.Plants (Basel, Switzerland) · 2023Review
- Spatial proteomics of vesicular trafficking: coupling mass spectrometry and imaging approaches in membrane biology.Plant biotechnology journal · 2023Review
- Pollen Coat Proteomes ofBiomolecules · 2023Article
- Semi-Supervised Non-Parametric Bayesian Modelling of Spatial Proteomics.The annals of applied statistics · 2022Article
- Polymerization of the backbone of the pectic polysaccharide rhamnogalacturonan I.Nature plants · 2022Article
- Eudicot primary cell wall glucomannan is related in synthesis, structure, and function to xyloglucan.The Plant cell · 2022Article
- Golgi-localized putative S-adenosyl methionine transporters required for plant cell wall polysaccharide methylation.Nature plants · 2022Article
- Subcellular Transcriptomics and Proteomics: A Comparative Methods Review.Molecular & cellular proteomics : MCP · 2022Review
- Golgi-localized membrane protein AtTMN1/EMP12 functions in the deposition of rhamnogalacturonan II and I for cell growth in Arabidopsis.Journal of experimental botany · 2021Article
- Subcellular Localization of Acyl-CoA: Lysophosphatidylethanolamine Acyltransferases (LPEATs) and the Effects of Knocking-Out and Overexpression of Their Genes on Autophagy Markers Level and Life Span ofInternational journal of molecular sciences · 2021Article
- A Pipeline towards the Biochemical Characterization of theInternational journal of molecular sciences · 2021Article
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- Subcellular Proteomics as a Unified Approach of Experimental Localizations and Computed Prediction Data for Arabidopsis and Crop Plants.Advances in experimental medicine and biology · 2021Article
- Subcellular proteomics.Nature reviews. Methods primers · 2021Article
- Characterization of In Vivo Function(s) of Members of the Plant Mitochondrial Carrier Family.Biomolecules · 2020Review
29 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The Golgi apparatus is the central organelle in the secretory pathway and plays key roles in glycosylation, protein sorting, and secretion in plants. Enzymes involved in the biosynthesis of complex polysaccharides, glycoproteins, and glycolipids are located in this organelle, but the majority of them remain uncharacterized. Here, we studied the Arabidopsis (Arabidopsis thaliana) membrane proteome with a focus on the Golgi apparatus using localization of organelle proteins by isotope tagging. By applying multivariate data analysis to a combined data set of two new and two previously published localization of organelle proteins by isotope tagging experiments, we identified the subcellular localization of 1,110 proteins with high confidence. These include 197 Golgi apparatus proteins, 79 of which have not been localized previously by a high-confidence method, as well as the localization of 304 endoplasmic reticulum and 208 plasma membrane proteins. Comparison of the hydrophobic domains of the localized proteins showed that the single-span transmembrane domains have unique properties in each organelle. Many of the novel Golgi-localized proteins belong to uncharacterized protein families. Structure-based homology analysis identified 12 putative Golgi glycosyltransferase (GT) families that have no functionally characterized members and, therefore, are not yet assigned to a Carbohydrate-Active Enzymes database GT family. The substantial numbers of these putative GTs lead us to estimate that the true number of plant Golgi GTs might be one-third above those currently annotated. Other newly identified proteins are likely to be involved in the transport and interconversion of nucleotide sugar substrates as well as polysaccharide and protein modification.
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