AI Article Synopsis
- A study investigated how mutations in the extracellular part of the TrkB receptor affect its ability to bind to brain-derived neurotrophic factor (BDNF).
- The deletion mutant TrkBDelta4 retained binding activities even with significant portions of its extracellular region removed, suggesting it can function similarly to the wild-type TrkB receptor.
- Results indicate that only the carboxyl-terminal half of the extracellular section of TrkB, specifically the Ig2 domain, is crucial for maintaining BDNF receptor functionality.
Article Abstract
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 (TrkBDelta4) 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 TrkBDelta4 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.
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| http://dx.doi.org/10.1016/s0005-2736(99)00094-2 | DOI Listing |
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