Cited by 8RNA Research and SplicingCellular transport and secretionFungal and yeast genetics research

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A MademoiseLLE domain binding platform links the key RNA transporter to endosomes

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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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Metadata

Authors
Devan, S.-K., Schott-Verdugo, S., Müntjes, K., Bismar, L., Reiners, J., Hachani, E., Schmitt, L., Höppner, A., Smits, S. H., Gohlke, H., & Feldbrügge, M.
Affiliations
  • Cluster of Excellence on Plant Sciences (DE)
  • Heinrich Heine University Düsseldorf (DE)
  • Forschungszentrum Jülich (DE)
Corresponding author
  • Devan, Senthil-Kumar
  • Müntjes, Kira
  • Bismar, Lilli
  • Reiners, Jens
  • Hachani, Eymen
  • Schmitt, Lutz
  • Smits, Sander HJ
  • Gohlke, Holger
  • Feldbrügge, Michael
Venue
PLOS Genetics
Published
2022-06-21
Volume
18
Issue
6
Pages
e1010269
ISSN
  • 1553-7390 (ISSN-L)
  • 1553-7404
OpenAlex
W4283265868
Cited by
8
References
2
Citations by year
2026: 1 · 2025: 2 · 2024: 2 · 2023: 3
FWCI
0.57
Type
journal article
Language
en
Open access
Locations
  • PLoS Genetics (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Deutsche Forschungsgemeinschaft (EXC-2048/1 - Project ID 39068111, Project-ID 267205415 – SFB 1208 A09, Project-ID 267205415 – SFB 1208 A03, Project-ID 267205415 – SFB 1208 A01, 417919780; INST 208/740-1 FUGG INST 208/761-1 FUGG)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
RNA-binding proteins, Ustilago maydis, structure-function analysis
MeSH terms
Fungal Proteins, Oligopeptides, Endosomes, RNA, RNA, Messenger, Ustilago, RNA-Binding Proteins, Membrane Transport Proteins, Toll-Like Receptor 2, Toll-Like Receptor 9

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