ArticlePLoS genetics2022
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes.
Article in PLoS genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Dissecting the RNA-binding capacity of the multi-RRM protein Rrm4 essential for endosomal mRNA transport.Nucleic acids research · 2026Article
- Vesicle-coupled mRNA transport and translation govern intracellular organelle networking.EMBO reports · 2026Review
- The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Microbial iCLIP2: enhanced mapping of RNA-protein interaction by promoting protein and RNA stability.RNA (New York, N.Y.) · 2025Article
- Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The RNA world of fungal pathogens.PLoS pathogens · 2023Article
- The mRNA stability factor Khd4 defines a specific mRNA regulon for membrane trafficking in the pathogenProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The IV International Symposium on Fungal Stress and the XIII International Fungal Biology Conference.Fungal biologyArticle
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spatiotemporal expression can be achieved by transport and translation of mRNAs at defined subcellular sites. An emerging mechanism mediating mRNA trafficking is microtubule-dependent co-transport on shuttling endosomes. Although progress has been made in identifying various components of the endosomal mRNA transport machinery, a mechanistic understanding of how these RNA-binding proteins are connected to endosomes is still lacking. Here, we demonstrate that a flexible MademoiseLLE (MLLE) domain platform within RNA-binding protein Rrm4 of Ustilago maydis is crucial for endosomal attachment. Our structure/function analysis uncovered three MLLE domains at the C-terminus of Rrm4 with a functionally defined hierarchy. MLLE3 recognises two PAM2-like sequences of the adaptor protein Upa1 and is essential for endosomal shuttling of Rrm4. MLLE1 and MLLE2 are most likely accessory domains exhibiting a variable binding mode for interaction with currently unknown partners. Thus, endosomal attachment of the mRNA transporter is orchestrated by a sophisticated MLLE domain binding platform.
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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.