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@ARTICLE{Devan:491345,
      author       = {Devan, Senthil-Kumar and Schott-Verdugo, Stephan and
                      Müntjes, Kira and Bismar, Lilli and Reiners, Jens and
                      Hachani, Eymen and Schmitt, Lutz and Höppner, Astrid and
                      Smits, Sander and Gohlke, Holger and Feldbrügge, Michael},
      title        = {{A} {M}ademoise{LLE} domain binding platform links the key
                      {RNA} transporter to endosomes},
      journal      = {PLoS Genetics},
      volume       = {18},
      number       = {6},
      issn         = {1553-7390},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {PUBDB-2023-00100},
      pages        = {e1010269},
      year         = {2022},
      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.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35727840},
      UT           = {WOS:000828680400007},
      doi          = {10.1371/journal.pgen.1010269},
      url          = {https://bib-pubdb1.desy.de/record/491345},
}