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@ARTICLE{Deyaert:139567,
      author       = {Deyaert, Egon and Wauters, Lina and Guaitoli, Giambattista
                      and Konijnenberg, Albert and Leemans, Margaux and Terheyden,
                      Susanne and Petrovic, Arsen and Gallardo, Rodrigo and
                      Nederveen-Schippers, Laura M and Athanasopoulos, Panagiotis
                      S and Pots, Henderikus and Van Haastert, Peter J M and
                      Sobott, Frank and Gloeckner, Christian Johannes and Efremov,
                      Rouslan and Kortholt, Arjan and Versées, Wim},
      title        = {{A} homologue of the {P}arkinson's disease-associated
                      protein {LRRK}2 undergoes a monomer-dimer transition during
                      {GTP} turnover.},
      journal      = {Nature Communications},
      volume       = {8},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2020-05889},
      pages        = {1008},
      year         = {2017},
      abstract     = {Mutations in LRRK2 are a common cause of genetic
                      Parkinson's disease (PD). LRRK2 is a multi-domain Roco
                      protein, harbouring kinase and GTPase activity. In analogy
                      with a bacterial homologue, LRRK2 was proposed to act as a
                      GTPase activated by dimerization (GAD), while recent reports
                      suggest LRRK2 to exist under a monomeric and dimeric form in
                      vivo. It is however unknown how LRRK2 oligomerization is
                      regulated. Here, we show that oligomerization of a
                      homologous bacterial Roco protein depends on the nucleotide
                      load. The protein is mainly dimeric in the nucleotide-free
                      and GDP-bound states, while it forms monomers upon GTP
                      binding, leading to a monomer-dimer cycle during GTP
                      hydrolysis. An analogue of a PD-associated mutation
                      stabilizes the dimer and decreases the GTPase activity. This
                      work thus provides insights into the conformational cycle of
                      Roco proteins and suggests a link between oligomerization
                      and disease-associated mutations in LRRK2.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      genetics / Bacterial Proteins: metabolism / Chlorobium:
                      chemistry / Chlorobium: enzymology / Chlorobium: genetics /
                      Dimerization / Guanosine Triphosphate: metabolism / Humans /
                      Hydrolysis / Leucine-Rich Repeat Serine-Threonine Protein
                      Kinase-2: chemistry / Leucine-Rich Repeat Serine-Threonine
                      Protein Kinase-2: genetics / Leucine-Rich Repeat
                      Serine-Threonine Protein Kinase-2: metabolism / Mutation /
                      Parkinson Disease: enzymology / Parkinson Disease: genetics
                      / Phosphorylation / Protein Structure, Tertiary / Bacterial
                      Proteins (NLM Chemicals) / Guanosine Triphosphate (NLM
                      Chemicals) / Leucine-Rich Repeat Serine-Threonine Protein
                      Kinase-2 (NLM Chemicals)},
      cin          = {AG Gloeckner},
      ddc          = {500},
      cid          = {I:(DE-2719)1210007},
      pnm          = {345 - Population Studies and Genetics (POF3-345)},
      pid          = {G:(DE-HGF)POF3-345},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29044096},
      pmc          = {pmc:PMC5714945},
      doi          = {10.1038/s41467-017-01103-4},
      url          = {https://pub.dzne.de/record/139567},
}