ArticleProtoplasma2014
Receptor-mediated transport of vacuolar proteins: a critical analysis and a new model.
Article in Protoplasma, 2014. 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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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components.The Plant cell · 2022Article
- Structural insights into how vacuolar sorting receptors recognize the sorting determinants of seed storage proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An Update on the Key Factors Required for Plant Golgi Structure Maintenance.Frontiers in plant science · 2022Review
- Transport, functions, and interaction of calcium and manganese in plant organellar compartments.Plant physiology · 2021Review
- Nanobody-triggered lockdown of VSRs reveals ligand reloading in the Golgi.Nature communications · 2018Article
- Vacuolar deposition of recombinant proteins in plant vegetative organs as a strategy to increase yields.Bioengineered · 2017Review
- Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017Review
- Vacuolar targeting of recombinant antibodies in Nicotiana benthamiana.Plant biotechnology journal · 2016Article
- Where do Protein Bodies of Cereal Seeds Come From?Frontiers in plant science · 2016Review
- Vacuolar Sorting Receptor-Mediated Trafficking of Soluble Vacuolar Proteins in Plant Cells.Plants (Basel, Switzerland) · 2014Review
- Trafficking of Vacuolar Sorting Receptors: New Data and New Problems.Plant physiology · 2014Article
- Activation of the Rab7 GTPase by the MON1-CCZ1 Complex Is Essential for PVC-to-Vacuole Trafficking and Plant Growth in Arabidopsis.The Plant cell · 2014Article
- Development and properties of genetically encoded pH sensors in plants.Frontiers in plant science · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this article we challenge the widely accepted view that receptors for soluble vacuolar proteins (VSRs) bind to their ligands at the trans-Golgi network (TGN) and transport this cargo via clathrin-coated vesicles (CCV) to a multivesicular prevacuolar compartment. This notion, which we term the "classical model" for vacuolar protein sorting, further assumes that low pH in the prevacuolar compartment causes VSR-ligand dissociation, resulting in a retromer-mediated retrieval of the VSRs to the TGN. We have carefully evaluated the literature with respect to morphology and function of the compartments involved, localization of key components of the sorting machinery, and conclude that there is little direct evidence in its favour. Firstly, unlike mammalian cells where the sorting receptor for lysosomal hydrolases recognizes its ligand in the TGN, the available data suggests that in plants VSRs interact with vacuolar cargo ligands already in the endoplasmic reticulum. Secondly, the evidence supporting the packaging of VSR-ligand complexes into CCV at the TGN is not conclusive. Thirdly, the prevacuolar compartment appears to have a pH unsuitable for VSR-ligand dissociation and lacks the retromer core and the sorting nexins needed for VSR recycling. We present an alternative model for protein sorting in the TGN that draws attention to the much overlooked role of Ca(2+) in VSR-ligand interactions and which may possibly also be a factor in the sequestration of secretory proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.