%0 Journal Article
%A Devan, Senthil-Kumar
%A Schott-Verdugo, Stephan
%A Müntjes, Kira
%A Bismar, Lilli
%A Reiners, Jens
%A Hachani, Eymen
%A Schmitt, Lutz
%A Höppner, Astrid
%A Smits, Sander HJ
%A Gohlke, Holger
%A Feldbrügge, Michael
%T A MademoiseLLE domain binding platform links the key RNA transporter to endosomes
%J PLoS Genetics
%V 18
%N 6
%@ 1553-7390
%C San Francisco, Calif.
%I Public Library of Science
%M FZJ-2022-03076
%P e1010269 -
%D 2022
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 35727840
%U <Go to ISI:>//WOS:000828680400007
%R 10.1371/journal.pgen.1010269
%U https://juser.fz-juelich.de/record/909232