Correction: Hsueh et al., 'Bipartite Interaction between Neurofibromatosis Type I Protein (Neurofibromin) and Syndecan Transmembrane Heparan Sulfate Proteoglycans'
| Autor: | Y P, Hsueh, A M, Roberts, M, Volta, M, Sheng, R G, Roberts |
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| Rok vydání: | 2017 |
| Předmět: |
congenital
hereditary and neonatal diseases and abnormalities Neurofibromatosis 1 Syndecans animal structures Macromolecular Substances Nerve Tissue Proteins Saccharomyces Two-Hybrid System Techniques Animals Humans ARTICLE Brain Chemistry Membrane Glycoproteins Neurofibromin 1 General Neuroscience Brain Correction Precipitin Tests Protein Structure Tertiary Rats nervous system diseases carbohydrates (lipids) Calcium-Calmodulin-Dependent Protein Kinases embryonic structures Syndecan-3 Proteoglycans Syndecan-2 Nucleoside-Phosphate Kinase Guanylate Kinases Heparan Sulfate Proteoglycans Protein Binding Subcellular Fractions |
| Zdroj: | The Journal of neuroscience : the official journal of the Society for Neuroscience. 37(5) |
| ISSN: | 1529-2401 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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