TY  - JOUR
AU  - Devan, Senthil-Kumar
AU  - Schott-Verdugo, Stephan
AU  - Müntjes, Kira
AU  - Bismar, Lilli
AU  - Reiners, Jens
AU  - Hachani, Eymen
AU  - Schmitt, Lutz
AU  - Höppner, Astrid
AU  - Smits, Sander HJ
AU  - Gohlke, Holger
AU  - Feldbrügge, Michael
TI  - A MademoiseLLE domain binding platform links the key RNA transporter to endosomes
JO  - PLoS Genetics
VL  - 18
IS  - 6
SN  - 1553-7390
CY  - San Francisco, Calif.
PB  - Public Library of Science
M1  - FZJ-2022-03076
SP  - e1010269 -
PY  - 2022
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 35727840
UR  - <Go to ISI:>//WOS:000828680400007
DO  - DOI:10.1371/journal.pgen.1010269
UR  - https://juser.fz-juelich.de/record/909232
ER  -