This title appears in the Scientific Report :
2022
Please use the identifier:
http://hdl.handle.net/2128/31670 in citations.
Please use the identifier: http://dx.doi.org/10.1371/journal.pgen.1010269 in citations.
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes
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 endoso...
Saved in:
Personal Name(s): | Devan, Senthil-Kumar |
---|---|
Schott-Verdugo, Stephan / Müntjes, Kira / Bismar, Lilli / Reiners, Jens / Hachani, Eymen / Schmitt, Lutz / Höppner, Astrid / Smits, Sander HJ (Corresponding author) / Gohlke, Holger (Corresponding author) / Feldbrügge, Michael (Corresponding author) | |
Contributing Institute: |
Bioinformatik; IBG-4 Strukturbiochemie; IBI-7 John von Neumann - Institut für Computing; NIC Jülich Supercomputing Center; JSC |
Published in: | PLoS Genetics, 18 (2022) 6, S. e1010269 - |
Imprint: |
San Francisco, Calif.
Public Library of Science
2022
|
DOI: |
10.1371/journal.pgen.1010269 |
Document Type: |
Journal Article |
Research Program: |
Molecular Information Processing in Cellular Systems Forschergruppe Gohlke Biological and environmental resources for sustainable use Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1371/journal.pgen.1010269 in citations.
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. |