@article{20351,
  abstract     = {Rab GTPases organize intracellular trafficking and provide identity to organelles. Their spatiotemporal activation by guanine nucleotide exchange factors (GEFs) is tightly controlled to ensure fidelity. Our structural and functional comparison of the tri-longin domain RabGEFs Mon1-Ccz1 and Fuzzy-Inturned reveals the molecular basis for their target specificity. Both complexes rely on a conserved sequence motif of their substrate GTPases for the catalytic mechanism, while secondary interactions allow discrimination between targets. We also find that dimeric Mon1-Ccz1 from fungi and the metazoan homologs with the additional third subunit RMC1/Bulli bind membranes through electrostatic interactions via distinct interfaces. Protein-lipid interaction studies and functional characterization in flies reveal an essential function of RMC1/Bulli as mediator of GEF complex membrane recruitment. In the case of Fuzzy-Inturned, reconstitution experiments demonstrate that the BAR (Bin-Amphiphysin-Rvs) domain protein CiBAR1 can support membrane recruitment of the GEF. Collectively, our study demonstrates the molecular basis for the adaptation of TLD-RabGEFs to different cellular functions.},
  author       = {Wilmes, Stephan and Tönjes, Jesse and Drechsler, Maik and Ruf, Anita and Schäfer, Jan Hannes and Lürick, Anna and Januliene, Dovile and Apelt, Steven and Di Iorio, Daniele and Wegner, Seraphine V. and Loose, Martin and Moeller, Arne and Paululat, Achim and Kümmel, Daniel},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {35},
  pages        = {eadx2893},
  publisher    = {AAAS},
  title        = {{Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned}},
  doi          = {10.1126/sciadv.adx2893},
  volume       = {11},
  year         = {2025},
}

@article{14039,
  abstract     = {Membranes are essential for life. They act as semi-permeable boundaries that define cells and organelles. In addition, their surfaces actively participate in biochemical reaction networks, where they confine proteins, align reaction partners, and directly control enzymatic activities. Membrane-localized reactions shape cellular membranes, define the identity of organelles, compartmentalize biochemical processes, and can even be the source of signaling gradients that originate at the plasma membrane and reach into the cytoplasm and nucleus. The membrane surface is, therefore, an essential platform upon which myriad cellular processes are scaffolded. In this review, we summarize our current understanding of the biophysics and biochemistry of membrane-localized reactions with particular focus on insights derived from reconstituted and cellular systems. We discuss how the interplay of cellular factors results in their self-organization, condensation, assembly, and activity, and the emergent properties derived from them.},
  author       = {Leonard, Thomas A. and Loose, Martin and Martens, Sascha},
  issn         = {1878-1551},
  journal      = {Developmental Cell},
  number       = {15},
  pages        = {1315--1332},
  publisher    = {Elsevier},
  title        = {{The membrane surface as a platform that organizes cellular and biochemical processes}},
  doi          = {10.1016/j.devcel.2023.06.001},
  volume       = {58},
  year         = {2023},
}