Bipartite interaction between neurofibromatosis type I protein (neurofibromin) and syndecan transmembrane heparan sulfate proteoglycans.

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  • Author(s): Hsueh YP;Hsueh YP; Roberts AM; Volta M; Sheng M; Roberts RG
  • Source:
    The Journal of neuroscience : the official journal of the Society for Neuroscience [J Neurosci] 2001 Jun 01; Vol. 21 (11), pp. 3764-70.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Society for Neuroscience Country of Publication: United States NLM ID: 8102140 Publication Model: Print Cited Medium: Internet ISSN: 1529-2401 (Electronic) Linking ISSN: 02706474 NLM ISO Abbreviation: J Neurosci Subsets: MEDLINE
    • Publication Information:
      Publication: Washington, DC : Society for Neuroscience
      Original Publication: [Baltimore, Md.] : The Society, c1981-
    • Subject Terms:
      Calcium-Calmodulin-Dependent Protein Kinases*; Heparan Sulfate Proteoglycans/*metabolism ; Membrane Glycoproteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Proteoglycans/*metabolism; Animals ; Brain/metabolism ; Brain Chemistry ; Guanylate Kinases ; Humans ; Macromolecular Substances ; Membrane Glycoproteins/genetics ; Nerve Tissue Proteins/genetics ; Neurofibromatosis 1/genetics ; Neurofibromin 1 ; Nucleoside-Phosphate Kinase/metabolism ; Precipitin Tests ; Protein Binding/physiology ; Protein Structure, Tertiary/physiology ; Proteoglycans/genetics ; Rats ; Saccharomyces/genetics ; Subcellular Fractions/chemistry ; Subcellular Fractions/metabolism ; Syndecan-2 ; Syndecan-3 ; Syndecans ; Two-Hybrid System Techniques
    • Abstract:
      The neurofibromatosis type 1 (NF1) gene encodes a large tumor suppressor protein (neurofibromin). Although it is known to possess Ras GTPase-activating protein (GAP) activity, the cellular role of neurofibromin remains unclear. Here we used yeast two-hybrid screening to identify neurofibromin-interacting proteins. Syndecan-2, a transmembrane heparan sulfate proteoglycan (HSPG), was isolated as a binding partner for two distinct regions of the neurofibromin protein. We subsequently found that neurofibromin can bind all four mammalian syndecans. NF1 interaction requires the transmembrane domain and a membrane-proximal region of the cytoplasmic tail of syndecan, but not the C terminus of syndecan known to bind to CASK, a membrane-associated guanylate kinase (MAGUK). Neurofibromin, syndecans, and CASK have overlapping subcellular distributions in axons and synapses of neurons, as shown by biochemical fractionation and immunostaining. Moreover, neurofibromin exists in a complex with syndecan and CASK in vivo, as evidenced by their coimmunoprecipitation from rat brain. Our findings suggest that interaction with different members of the syndecan family may be a mechanism for localizing neurofibromin to specialized domains of the plasma membrane.
    • Comments:
      Erratum in: J Neurosci. 2017 Feb 1;37(5):1374. (PMID: 28148807)
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    • Grant Information:
      United Kingdom Wellcome Trust
    • Accession Number:
      0 (Heparan Sulfate Proteoglycans)
      0 (Macromolecular Substances)
      0 (Membrane Glycoproteins)
      0 (Nerve Tissue Proteins)
      0 (Neurofibromin 1)
      0 (Proteoglycans)
      0 (SDC2 protein, human)
      0 (SDC3 protein, human)
      0 (Sdc2 protein, rat)
      0 (Sdc3 protein, rat)
      0 (Syndecan-3)
      0 (Syndecans)
      149769-25-5 (Syndecan-2)
      EC 2.7.11.1 (CASK kinases)
      EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
      EC 2.7.4.4 (Nucleoside-Phosphate Kinase)
      EC 2.7.4.8 (Guanylate Kinases)
    • Publication Date:
      Date Created: 20010523 Date Completed: 20010621 Latest Revision: 20191023
    • Publication Date:
      20231215
    • Accession Number:
      PMC6762697
    • Accession Number:
      11356864