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001     491345
005     20250724152202.0
024 7 _ |a 10.1371/journal.pgen.1010269
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082 _ _ |a 610
100 1 _ |a Devan, Senthil-Kumar
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245 _ _ |a A MademoiseLLE domain binding platform links the key RNA transporter to endosomes
260 _ _ |a San Francisco, Calif.
|c 2022
|b Public Library of Science
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520 _ _ |a 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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700 1 _ |a Schott-Verdugo, Stephan
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700 1 _ |a Müntjes, Kira
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700 1 _ |a Bismar, Lilli
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700 1 _ |a Reiners, Jens
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700 1 _ |a Hachani, Eymen
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700 1 _ |a Schmitt, Lutz
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700 1 _ |a Höppner, Astrid
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700 1 _ |a Smits, Sander
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700 1 _ |a Gohlke, Holger
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700 1 _ |a Feldbrügge, Michael
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773 _ _ |a 10.1371/journal.pgen.1010269
|g Vol. 18, no. 6, p. e1010269 -
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|t PLoS Genetics
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|y 2022
|x 1553-7390
856 4 _ |u https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1010269
856 4 _ |u https://bib-pubdb1.desy.de/record/491345/files/A%20MademoiseLLE%20domain%20binding%20platform%20links%20the%20key%20RNA%20transporter%20to%20endosomes.pdf
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