Abstract
To investigate the role of Bone Morphogenic Protein Receptor Type II (BMPRII) in learning, memory, and exploratory behavior in mice, a tissue-specific knockout of BMPRII in the post-natal hippocampus and forebrain was generated. We found that BMPRII mutant mice had normal spatial learning and memory in the Morris water maze, but showed significantly reduced swimming speeds with increased floating behavior. Further analysis using the Porsolt Swim Test to investigate behavioral despair did not reveal any differences in immobility between mutants and controls. In the Elevated Plus Maze, BMPRII mutants and Smad4 mutants showed reduced anxiety, while in exploratory tests, BMPRII mutants showed more interest in object exploration. These results suggest that loss of BMPRII in the mouse hippocampus and forebrain does not disrupt spatial learning and memory encoding, but instead impacts exploratory and anxiety-related behaviors.
Highlights
Bone Morphogenic Proteins (BMPs) form the largest subclass of secreted signaling factors within the TGF-β (Transforming Growth Factor) superfamily
In order to investigate the role of BMP signaling in learning and memory, we generated a tissue-specific knockout of Bone Morphogenic Protein Receptor Type II (BMPRII) in the postnatal hippocampus and forebrain using the L7ag#13 line of CaMKIIα-Cre to delete a floxed allele of BMPRII [25] beginning at postnatal day 5 [26,27]
Our studies indicate that fbΔBMPRII mutant mice show reduced anxiety-like behavior and increased exploratory behavior
Summary
Bone Morphogenic Proteins (BMPs) form the largest subclass of secreted signaling factors within the TGF-β (Transforming Growth Factor) superfamily. These factors control a plethora of developmental and homostatic processes in higher eurkayotes including, axial development, tissue patterning, wound healing, immune regulation and apoptotic responses. BMP ligands form homeomeric or heteromeric dimers that bind to type I (BMPRIA or BMPRIB) and type II (BMPRII, ACTRII, and ACTRIIB) receptors. Ligand binding stabilizes the interaction between type I and type II receptors, which allows phosphorylation of the GS domain in the type I receptor by the constitutively active kinase domain of the type II receptor. After phosphorylation by the activated receptor complex, the activated R-Smads partner with a common Smad (Smad 4), and the stabilized complex accumulates in the nucleus
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