PreprintCited by 0RNA 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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Devan, Senthil-Kumar, Schott-Verdugo, Stephan, Müntjes, Kira, Bismar, Lilli, Reiners, Jens, Hachani, Eymen, Schmitt, Lutz, Höppner, Astrid, Smits, Sander HJ, Gohlke, Holger, Feldbrügge, Michael·2021·bioRxiv (Cold Spring Harbor Laboratory)

Preprint — published as 10.1371/journal.pgen.1010269 · Paper page

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
  • Smits, Sander HJ
  • Gohlke, Holger
  • Feldbrügge, Michael
Venue
bioRxiv (Cold Spring Harbor Laboratory)
Publisher
openRxiv
Published
2021-10-25
OpenAlex
W3211005898
Cited by
0
References
1
Type
posted content
Language
en
Open access
Licence
cc-by-nc
Locations
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (submittedVersion, other-oa)
Funders
  • Deutsche Forschungsgemeinschaft (project A01), SFB 1208, Project A03, EXC-2048, EXC-2048/1, 267205415, INST 208/740‐1 FUGG, INST 208/761‐1 FUGG, 39068111, 417919780, 2048/1)
  • European Synchrotron Radiation Facility
  • Heinrich-Heine-Universität Düsseldorf
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

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