ArticleJournal of experimental botany2016
The Arabidopsis tonoplast is almost devoid of glycoproteins with complex N-glycans, unlike the rat lysosomal membrane.
Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 22 citations in OpenAlex.
- A dual phospholipase system instructs membrane hydrolysis during the final stages of plant autophagy.Nature communications · 2026Article
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- Glycosylation Analysis of Feline Small Intestine FollowingAnimals : an open access journal from MDPI · 2022Article
- Current Methods to Unravel the Functional Properties of Lysosomal Ion Channels and Transporters.Cells · 2022Review
- Identification of MAMP-Responsive Plasma Membrane-Associated Proteins inPathogens (Basel, Switzerland) · 2020Article
- A Review of Plant Vacuoles: Formation, Located Proteins, and Functions.Plants (Basel, Switzerland) · 2019Review
- Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1.Frontiers in plant science · 2018Article
- Protein and membrane trafficking routes in plants: conventional or unconventional?Journal of experimental botany · 2017Article
- Glutathione S-transferase related detoxification processes are correlated with receptor-mediated vacuolar sorting mechanisms.Plant cell reports · 2017Article
- Unconventional Transport Routes of Soluble and Membrane Proteins and Their Role in Developmental Biology.International journal of molecular sciences · 2017Article
- Evolution of protein N-glycosylation process in Golgi apparatus which shapes diversity of protein N-glycan structures in plants, animals and fungi.Scientific reports · 2017Article
- Experimental botany in 2017.Journal of experimental botany · 2017Article
- The tonoplast--where sweetness is dispensable.Journal of experimental botany · 2016Article
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8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The distribution of the N-glycoproteome in integral membrane proteins of the vacuolar membrane (tonoplast) or the plasma membrane of Arabidopsis thaliana and, for further comparison, of the Rattus norvegicus lysosomal and plasma membranes, was analyzed. In silico analysis showed that potential N-glycosylation sites are much less frequent in tonoplast proteins. Biochemical analysis of Arabidopsis subcellular fractions with the lectin concanavalin A, which recognizes mainly unmodified N-glycans, or with antiserum against Golgi-modified N-glycans confirmed the in silico results and showed that, unlike the plant plasma membrane, the tonoplast is almost or totally devoid of N-glycoproteins with Golgi-modified glycans. Lysosomes share with vacuoles the hydrolytic functions and the position along the secretory pathway; however, our results indicate that their membranes had a divergent evolution. We propose that protection against the luminal hydrolases that are abundant in inner hydrolytic compartments, which seems to have been achieved in many lysosomal membrane proteins by extensive N-glycosylation of the luminal domains, has instead been obtained in the vast majority of tonoplast proteins by limiting the length of such domains.
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