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000141300 0247_ $$2doi$$a10.1038/ncomms6209
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000141300 041__ $$aEnglish
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000141300 1001_ $$0P:(DE-2719)2810781$$aColes, Charlotte H$$b0$$eFirst author$$udzne
000141300 245__ $$aStructural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis.
000141300 260__ $$a[London]$$bNature Publishing Group UK$$c2014
000141300 264_1 $$2Crossref$$3online$$bSpringer Science and Business Media LLC$$c2014-11-11
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000141300 520__ $$aReceptor protein tyrosine phosphatase sigma (RPTPσ) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan interactions during synaptogenesis. Unknown mechanisms govern the shift in RPTPσ function, from outgrowth promotion to synaptic organization. Here, we report crystallographic, electron microscopic and small-angle X-ray scattering analyses, which reveal sufficient inter-domain flexibility in the RPTPσ extracellular region for interaction with both cis (same cell) and trans (opposite cell) ligands. Crystal structures of RPTPσ bound to its postsynaptic ligand TrkC detail an interaction surface partially overlapping the glycosaminoglycan-binding site. Accordingly, heparan sulphate and heparin oligomers compete with TrkC for RPTPσ binding in vitro and disrupt TrkC-dependent synaptic differentiation in neuronal co-culture assays. We propose that transient RPTPσ ectodomain emergence from the presynaptic proteoglycan layer allows capture by TrkC to form a trans-synaptic complex, the consequent reduction in RPTPσ flexibility potentiating interactions with additional ligands to orchestrate excitatory synapse formation.
000141300 536__ $$0G:(DE-HGF)POF3-341$$a341 - Molecular Signaling (POF3-341)$$cPOF3-341$$fPOF III$$x0
000141300 542__ $$2Crossref$$i2014-11-11$$uhttps://creativecommons.org/licenses/by/4.0
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000141300 650_7 $$2NLM Chemicals$$aExtracellular Matrix Proteins
000141300 650_7 $$2NLM Chemicals$$aLigands
000141300 650_7 $$2NLM Chemicals$$aProteoglycans
000141300 650_7 $$0EC 2.7.10.1$$2NLM Chemicals$$aReceptor, trkC
000141300 650_7 $$0EC 3.1.3.48$$2NLM Chemicals$$aReceptor-Like Protein Tyrosine Phosphatases, Class 2
000141300 650_2 $$2MeSH$$aAnimals
000141300 650_2 $$2MeSH$$aCell Differentiation: physiology
000141300 650_2 $$2MeSH$$aChick Embryo
000141300 650_2 $$2MeSH$$aCoculture Techniques
000141300 650_2 $$2MeSH$$aCrystallization
000141300 650_2 $$2MeSH$$aExtracellular Matrix Proteins: chemistry
000141300 650_2 $$2MeSH$$aExtracellular Matrix Proteins: physiology
000141300 650_2 $$2MeSH$$aHumans
000141300 650_2 $$2MeSH$$aLigands
000141300 650_2 $$2MeSH$$aMice
000141300 650_2 $$2MeSH$$aNeurogenesis: physiology
000141300 650_2 $$2MeSH$$aNeurons: cytology
000141300 650_2 $$2MeSH$$aNeurons: physiology
000141300 650_2 $$2MeSH$$aProtein Binding
000141300 650_2 $$2MeSH$$aProtein Structure, Tertiary
000141300 650_2 $$2MeSH$$aProteoglycans: chemistry
000141300 650_2 $$2MeSH$$aProteoglycans: physiology
000141300 650_2 $$2MeSH$$aReceptor, trkC: chemistry
000141300 650_2 $$2MeSH$$aReceptor, trkC: physiology
000141300 650_2 $$2MeSH$$aReceptor-Like Protein Tyrosine Phosphatases, Class 2: chemistry
000141300 650_2 $$2MeSH$$aReceptor-Like Protein Tyrosine Phosphatases, Class 2: physiology
000141300 650_2 $$2MeSH$$aSignal Transduction: physiology
000141300 650_2 $$2MeSH$$aSynapses: physiology
000141300 7001_ $$aMitakidis, Nikolaos$$b1
000141300 7001_ $$aZhang, Peng$$b2
000141300 7001_ $$aElegheert, Jonathan$$b3
000141300 7001_ $$aLu, Weixian$$b4
000141300 7001_ $$aStoker, Andrew W$$b5
000141300 7001_ $$aNakagawa, Terunaga$$b6
000141300 7001_ $$aCraig, Ann Marie$$b7
000141300 7001_ $$0P:(DE-HGF)0$$aJones, E Yvonne$$b8$$eCorresponding author
000141300 7001_ $$aAricescu, A Radu$$b9
000141300 77318 $$2Crossref$$3journal-article$$a10.1038/ncomms6209$$b : Springer Science and Business Media LLC, 2014-11-11$$n1$$p5209$$tNature Communications$$v5$$x2041-1723$$y2014
000141300 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/ncomms6209$$gVol. 5, no. 1, p. 5209$$n1$$p5209$$q5:1<5209$$tNature Communications$$v5$$x2041-1723$$y2014
000141300 8564_ $$uhttps://www.nature.com/articles/ncomms6209
000141300 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4239663
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