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    Proteoglycan-specific molecular switch for RPTPσ clustering and neuronal extension.

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    Authors
    Coles, Charlotte H
    Shen, Yingjie
    Tenney, Alan P
    Siebold, Christian
    Sutton, Geoffrey C
    Lu, Weixian
    Gallagher, John T
    Jones, E Yvonne
    Flanagan, John G
    Aricescu, A Radu
    Affiliation
    Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.
    Issue Date
    2011-04-22
    
    Metadata
    Show full item record
    Abstract
    Heparan and chondroitin sulfate proteoglycans (HSPGs and CSPGs, respectively) regulate numerous cell surface signaling events, with typically opposite effects on cell function. CSPGs inhibit nerve regeneration through receptor protein tyrosine phosphatase sigma (RPTPσ). Here we report that RPTPσ acts bimodally in sensory neuron extension, mediating CSPG inhibition and HSPG growth promotion. Crystallographic analyses of a shared HSPG-CSPG binding site reveal a conformational plasticity that can accommodate diverse glycosaminoglycans with comparable affinities. Heparan sulfate and analogs induced RPTPσ ectodomain oligomerization in solution, which was inhibited by chondroitin sulfate. RPTPσ and HSPGs colocalize in puncta on sensory neurons in culture, whereas CSPGs occupy the extracellular matrix. These results lead to a model where proteoglycans can exert opposing effects on neuronal extension by competing to control the oligomerization of a common receptor.
    Citation
    Proteoglycan-specific molecular switch for RPTPσ clustering and neuronal extension. 2011, 332 (6028):484-8 Science
    Journal
    Science
    URI
    http://hdl.handle.net/10541/202460
    DOI
    10.1126/science.1200840
    PubMed ID
    21454754
    Type
    Article
    Language
    en
    ISSN
    1095-9203
    ae974a485f413a2113503eed53cd6c53
    10.1126/science.1200840
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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