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@ARTICLE{Coles:141300,
      author       = {Coles, Charlotte H and Mitakidis, Nikolaos and Zhang, Peng
                      and Elegheert, Jonathan and Lu, Weixian and Stoker, Andrew W
                      and Nakagawa, Terunaga and Craig, Ann Marie and Jones, E
                      Yvonne and Aricescu, A Radu},
      title        = {{S}tructural basis for extracellular cis and trans {RPTP}σ
                      signal competition in synaptogenesis.},
      journal      = {Nature Communications},
      volume       = {5},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2020-07622},
      pages        = {5209},
      year         = {2014},
      abstract     = {Receptor protein tyrosine phosphatase sigma (RPTPσ)
                      regulates neuronal extension and acts as a presynaptic nexus
                      for multiple protein and proteoglycan interactions during
                      synaptogenesis. Unknown mechanisms govern the shift in
                      RPTPσ function, from outgrowth promotion to synaptic
                      organization. Here, we report crystallographic, electron
                      microscopic and small-angle X-ray scattering analyses, which
                      reveal sufficient inter-domain flexibility in the RPTPσ
                      extracellular region for interaction with both cis (same
                      cell) and trans (opposite cell) ligands. Crystal structures
                      of RPTPσ bound to its postsynaptic ligand TrkC detail an
                      interaction surface partially overlapping the
                      glycosaminoglycan-binding site. Accordingly, heparan
                      sulphate and heparin oligomers compete with TrkC for RPTPσ
                      binding in vitro and disrupt TrkC-dependent synaptic
                      differentiation in neuronal co-culture assays. We propose
                      that transient RPTPσ ectodomain emergence from the
                      presynaptic proteoglycan layer allows capture by TrkC to
                      form a trans-synaptic complex, the consequent reduction in
                      RPTPσ flexibility potentiating interactions with additional
                      ligands to orchestrate excitatory synapse formation.},
      keywords     = {Animals / Cell Differentiation: physiology / Chick Embryo /
                      Coculture Techniques / Crystallization / Extracellular
                      Matrix Proteins: chemistry / Extracellular Matrix Proteins:
                      physiology / Humans / Ligands / Mice / Neurogenesis:
                      physiology / Neurons: cytology / Neurons: physiology /
                      Protein Binding / Protein Structure, Tertiary /
                      Proteoglycans: chemistry / Proteoglycans: physiology /
                      Receptor, trkC: chemistry / Receptor, trkC: physiology /
                      Receptor-Like Protein Tyrosine Phosphatases, Class 2:
                      chemistry / Receptor-Like Protein Tyrosine Phosphatases,
                      Class 2: physiology / Signal Transduction: physiology /
                      Synapses: physiology / Extracellular Matrix Proteins (NLM
                      Chemicals) / Ligands (NLM Chemicals) / Proteoglycans (NLM
                      Chemicals) / Receptor, trkC (NLM Chemicals) / Receptor-Like
                      Protein Tyrosine Phosphatases, Class 2 (NLM Chemicals)},
      cin          = {AG Bradke},
      ddc          = {500},
      cid          = {I:(DE-2719)1013002},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25385546},
      pmc          = {pmc:PMC4239663},
      doi          = {10.1038/ncomms6209},
      url          = {https://pub.dzne.de/record/141300},
}