TrkB mutant lacking the amino-terminal half of the extracellular portion acts as a functional brain-derived neurotrophic factor receptor
| Autor: | Satoshi Kojima, Goro Kuwajima, Harukazu Suzuki, Tsuneaki Sakata, Takashi Nakayama |
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| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Biophysics Tyrosine kinase receptor Tropomyosin receptor kinase B Receptors Nerve Growth Factor Tropomyosin receptor kinase A In Vitro Techniques Biochemistry Tropomyosin receptor kinase C Receptor tyrosine kinase Mice Neurotrophic factors Deletion mutant Extracellular Low-affinity nerve growth factor receptor Animals Receptor Ciliary Neurotrophic Factor Ligand binding Sequence Deletion Binding Sites biology musculoskeletal neural and ocular physiology Brain-Derived Neurotrophic Factor Receptor Protein-Tyrosine Kinases Cell Biology 3T3 Cells Molecular biology Peptide Fragments Recombinant Proteins nervous system embryonic structures COS Cells biology.protein Neurotrophin Immunoglobulin-like domain |
| Zdroj: | Biochimica et biophysica acta. 1420(1-2) |
| ISSN: | 0006-3002 |
| Popis: | A series of mutants with deletion in the extracellular portion of TrkB were expressed transiently and stably in mammalian cells to examine the brain-derived neurotrophic factor (BDNF)-binding properties of TrkB. We found that these binding activities were retained by the TrkB deletion mutant (TrkBΔ4) lacking most of the extracellular portion, cysteine-rich cluster 1 and 2, leucine-rich motif and most of the first immunoglobulin-like domain (Ig1). Furthermore, the results of the neurotrophin selectivity, the equilibrium binding constant, auto-phosphorylation and BDNF dependent cell survival indicate that TrkBΔ4 acts as a functional BDNF receptor comparable to wild-type TrkB. Thus, our findings showed that only the carboxyl-terminal half of the extracellular portion of TrkB, which includes the Ig2 domain, is essential for the functional BDNF receptor. |
| Databáze: | OpenAIRE |
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