AI Article Synopsis
- The neurotrophin BDNF and its receptor TrkB are key players in neuronal functions vital for learning and memory, particularly through synaptic plasticity.
- When BDNF binds to TrkB, it undergoes tyrosine and serine phosphorylation, but the role of the serine phosphorylation at S478 was previously unclear.
- Research using mice lacking this specific phosphorylation revealed that it is essential for spatial memory and long-term potentiation, highlighting its critical role in dendritic spine remodeling and overall cognitive function.
Article Abstract
The neurotrophin brain-derived neurotrophic factor (BDNF) and its receptor TrkB participate in diverse neuronal functions, including activity-dependent synaptic plasticity that is crucial for learning and memory. On binding to BDNF, TrkB is not only autophosphorylated at tyrosine residues but also undergoes serine phosphorylation at S478 by the serine/threonine kinase cyclin-dependent kinase 5 (Cdk5). However, the in vivo function of this serine phosphorylation remains unknown. We generated knock-in mice lacking this serine phosphorylation (Trkb(S478A/S478A) mice) and found that the TrkB phosphorylation-deficient mice displayed impaired spatial memory and compromised hippocampal long-term potentiation (LTP). S478 phosphorylation of TrkB regulates its interaction with the Rac1-specific guanine nucleotide exchange factor TIAM1, leading to activation of Rac1 and phosphorylation of S6 ribosomal protein during activity-dependent dendritic spine remodeling. These findings reveal the importance of Cdk5-mediated S478 phosphorylation of TrkB in activity-dependent structural plasticity, which is crucial for LTP and spatial memory formation.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7511999 | PMC |
| http://dx.doi.org/10.1038/nn.3237 | DOI Listing |
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