ArticlePlant signaling & behavior2013
Retromer association with membranes: plants have their own rules!
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- EhVps35, a retromer component, is involved in the recycling of the EhADH and Gal/GalNac virulent proteins ofFrontiers in parasitology · 2024Article
- Diversity of retromer-mediated vesicular trafficking pathways in plants.Frontiers in plant science · 2023Review
- G-Protein Phosphorylation: Aspects of Binding Specificity and Function in the Plant Kingdom.International journal of molecular sciences · 2022Review
- Remove, Recycle, Degrade: Regulating Plasma Membrane Protein Accumulation.The Plant cell · 2019Review
- Interaction between VPS35 and RABG3f is necessary as a checkpoint to control fusion of late compartments with the vacuole.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Updated Insight into the Physiological and Pathological Roles of the Retromer Complex.International journal of molecular sciences · 2017Review
- Resolving the homology-function relationship through comparative genomics of membrane-trafficking machinery and parasite cell biology.Molecular and biochemical parasitologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The retromer is an endosome-localized complex involved in protein trafficking. To better understand its function and regulation in plants, we recently investigated how Arabidopsis retromer subunits assemble and are targeted to endosomal membranes and highlighted original features compared with mammals. We characterized Arabidopsis vps26 null mutant and showed that it displays severe developmental defaults similar to those observed in vps29 mutant. Here, we go further by describing new phenotypic defects associated with loss of VPS26 function, such as inhibition of lateral root initiation. Recently, we showed that VPS35 subunit plays a crucial role in the recruitment of the plant retromer to endosomes, probably through an interaction with the Rab7 homolog RABG3f. In this work, we now show that contrary to mammals, Arabidopsis Rab5 homologs do not seem to be necessary for the recruitment of the core retromer to endosomal membranes, which highlights a new specificity of the plant retromer.
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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.