@article{12163,
  abstract     = {Small GTPases play essential roles in the organization of eukaryotic cells. In recent years, it has become clear that their intracellular functions result from intricate biochemical networks of the GTPase and their regulators that dynamically bind to a membrane surface. Due to the inherent complexities of their interactions, however, revealing the underlying mechanisms of action is often difficult to achieve from in vivo studies. This review summarizes in vitro reconstitution approaches developed to obtain a better mechanistic understanding of how small GTPase activities are regulated in space and time.},
  author       = {Loose, Martin and Auer, Albert and Brognara, Gabriel and Budiman, Hanifatul R and Kowalski, Lukasz M and Matijevic, Ivana},
  issn         = {1873-3468},
  journal      = {FEBS Letters},
  keywords     = {Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics},
  number       = {6},
  pages        = {762--777},
  publisher    = {Wiley},
  title        = {{In vitro reconstitution of small GTPase regulation}},
  doi          = {10.1002/1873-3468.14540},
  volume       = {597},
  year         = {2023},
}

@article{15036,
  abstract     = {The assembly of a septin filament requires that homologous monomers must distinguish between one another in establishing appropriate interfaces with their neighbors. To understand this phenomenon at the molecular level, we present the first four crystal structures of heterodimeric septin complexes. We describe in detail the two distinct types of G-interface present within the octameric particles, which must polymerize to form filaments. These are formed between SEPT2 and SEPT6 and between SEPT7 and SEPT3, and their description permits an understanding of the structural basis for the selectivity necessary for correct filament assembly. By replacing SEPT6 by SEPT8 or SEPT11, it is possible to rationalize Kinoshita's postulate, which predicts the exchangeability of septins from within a subgroup. Switches I and II, which in classical small GTPases provide a mechanism for nucleotide-dependent conformational change, have been repurposed in septins to play a fundamental role in molecular recognition. Specifically, it is switch I which holds the key to discriminating between the two different G-interfaces. Moreover, residues which are characteristic for a given subgroup play subtle, but pivotal, roles in guaranteeing that the correct interfaces are formed.},
  author       = {Rosa, Higor Vinícius Dias and Leonardo, Diego Antonio and Brognara, Gabriel and Brandão-Neto, José and D'Muniz Pereira, Humberto and Araújo, Ana Paula Ulian and Garratt, Richard Charles},
  issn         = {0022-2836},
  journal      = {Journal of Molecular Biology},
  keywords     = {Molecular Biology, Structural Biology},
  number       = {21},
  pages        = {5784--5801},
  publisher    = {Elsevier},
  title        = {{Molecular recognition at septin interfaces: The switches hold the key}},
  doi          = {10.1016/j.jmb.2020.09.001},
  volume       = {432},
  year         = {2020},
}