ArticleThe Plant cell2016
ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis.
Article in The Plant cell, 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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Who cites it
13 citing papers in PubMed.
- REAP1/AtSWAP70 integrates RAB5 and ROP signalling during sexual reproduction.Nature plants · 2026Article
- RAB GTPases and SNAREs at the trans-Golgi network in plants.Journal of plant research · 2022Review
- Creativity comes from interactions: modules of protein interactions in plants.The FEBS journal · 2022Review
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- The Golgi Apparatus and its Next-Door Neighbors.Frontiers in cell and developmental biology · 2022Review
- Inhibition of Very Long Chain Fatty Acids Synthesis Mediates PI3P Homeostasis at Endosomal Compartments.International journal of molecular sciences · 2021Article
- Attracted to membranes: lipid-binding domains in plants.Plant physiology · 2021Article
- Comparative Inter- and IntraSpecies Transcriptomics Revealed Key Differential Pathways Associated With Aluminium Stress Tolerance in Lentil.Frontiers in plant science · 2021Article
- MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Evolutionary insights into FYVE and PHOX effector proteins from the moss Physcomitrella patens.Planta · 2020Article
- Article
- Localization of Arabidopsis FORKED1 to a RABA-positive compartment suggests a role in secretion.Journal of experimental botany · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RAB5 GTPases act as molecular switches that regulate various endosomal functions in animal cells, including homotypic fusion of early endosomes, endosomal motility, endosomal signaling, and subcompartmentalization of the endosomal membrane. RAB5 proteins fulfill these diverse functions through interactions with downstream effector molecules. Two canonical RAB5 members, ARA7 and RAB HOMOLOG1 (RHA1), are encoded in the Arabidopsis thaliana genome. ARA7 and RHA1 play crucial roles in endocytic and vacuolar trafficking pathways. Plant RAB5 GTPases function via interactions with effector molecules, whose identities and functions are currently unclear. In this study, we searched for canonical RAB5 effector molecules of Arabidopsis and identified a candidate, which we called ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN (EREX). The intimate genetic interaction between EREX and RAB5 members, the results from subcellular colocalization experiments, and the direct interaction observed in an in vitro pull-down assay strongly suggest that EREX is a genuine effector of canonical RAB5s in Arabidopsis. We further found that close homologs of EREX play partially redundant functions with EREX in the transport of seed storage proteins. Our results indicate that canonical plant RAB5s acquired distinct effector molecules from those of non-plant systems to fulfill their functions.
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