ArticleeLife2015
A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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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.
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Who cites it
57 citing papers in PubMed, 108 citations in OpenAlex.
- ZNF512B associates with mitotic spindles, regulates metaphase exit, and is crucial for stem cell differentiation.Nucleic acids research · 2026Article
- Vesicle-coupled mRNA transport and translation govern intracellular organelle networking.EMBO reports · 2026Review
- Acyl-CoA-binding protein AcbdA is required for peroxisome hitchhiking on early endosomes inMolecular biology of the cell · 2025Article
- Condensate-membrane interactions shape membranes, tune cytoskeletal assembly, and localize mRNAs.Current opinion in cell biology · 2025Review
- Extracellular Vesicular Delta-Like Ligand 3 and Subtype Transcription Factors for Small Cell Lung Cancer Diagnosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- ZNF512B binds RBBP4 via a variant NuRD interaction motif and aggregates chromatin in a NuRD complex-independent manner.Nucleic acids research · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.Cell reports · 2024Article
- Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dynamic interaction of REEP5-MFN1/2 enables mitochondrial hitchhiking on tubular ER.The Journal of cell biology · 2024Article
- Nanoscale dynamics and localization of single endogenous mRNAs in stress granules.Nucleic acids research · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024Article
- Arabidopsis cyclophilins direct intracellular transport of mobile mRNA via organelle hitchhiking.Nature plants · 2024Article
- RNA-binding is an ancient trait of the Annexin family.Frontiers in cell and developmental biology · 2023Article
- mRNA Localization to the Endoplasmic Reticulum in Plant Endosperm Cells.International journal of molecular sciences · 2022Review
- Hitchhiking Across Kingdoms: Cotransport of Cargos in Fungal, Animal, and Plant Cells.Annual review of cell and developmental biology · 2022Review
- Distinct Mechanisms of Endomembrane Reorganization Determine Dissimilar Transport Pathways in Plant RNA Viruses.Plants (Basel, Switzerland) · 2022Review
- Bioinformatic Analysis Predicts a Novel Genetic Module Related to Triple Gene and Binary Movement Blocks of Plant Viruses: Tetra-Cistron Movement Block.Biomolecules · 2022Article
- A MademoiseLLE domain binding platform links the key RNA transporter to endosomes.PLoS genetics · 2022Article
- The Interplay Between Autophagy and RNA Homeostasis: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia.Frontiers in cell and developmental biology · 2022Review
- Linking transport and translation of mRNAs with endosomes and mitochondria.EMBO reports · 2021Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An emerging theme in cellular logistics is the close connection between mRNA and membrane trafficking. A prominent example is the microtubule-dependent transport of mRNAs and associated ribosomes on endosomes. This coordinated process is crucial for correct septin filamentation and efficient growth of polarised cells, such as fungal hyphae. Despite detailed knowledge on the key RNA-binding protein and the molecular motors involved, it is unclear how mRNAs are connected to membranes during transport. Here, we identify a novel factor containing a FYVE zinc finger domain for interaction with endosomal lipids and a new PAM2-like domain required for interaction with the MLLE domain of the key RNA-binding protein. Consistently, loss of this FYVE domain protein leads to specific defects in mRNA, ribosome, and septin transport without affecting general functions of endosomes or their movement. Hence, this is the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mRNPs to endosomes.
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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.