Most brain functions, such as memory, require a sophisticated network of molecular interactions. However, experimental methods can only analyze a limited number of these interactions at a time.
Now, researchers have pioneered a novel approach, which enables them to analyze hundreds of network molecules simultaneously. Ralf Schoepfer, Al Burlingame and colleagues were able to compare the relative amount and, importantly, the phosphorylation status of proteins in the synapses of four different brain regions.
Synapses are the traffic intersections in our brain, the junctions between neurons where one cell passes information to its neighbor.
To better understand this flow of traffic, the scientists used mass spectrometry tools to analyze the post-synaptic density (PSD, the synapses' receiving end) of four brain regions in mice: cortex, midbrain, cerebellum, and hippocampus. In total, they examined over 2000 proteins and found some telling data about neuronal transmissions and memory.
For example, they observed that of all the brain regions, the hippocampus contained the highest levels of kinases and phosphatases, proteins that add and remove phosphate tags from other proteins. Phosphorylation provides a flexible and easily reversible way to regulate proteins, and this revelation suggests this may be how the hippocampus carries out one of its' main duties: collecting and consolidating memories.
This novel analysis should greatly aid efforts to understand how different parts of the brain handle their different jobs, and will also provides opportunities to investigate neuronal repair mechanisms and diseases such as Autism or Schizophrenia.
Journal reference: "Quantitative Analysis of Synaptic Phosphorylation and Protein Expression" by JC Trinidad, A Thalhammer, CG Specht, AJ Lynn, PR Baker, R Schoepfer, and AL Burlingame.Molecular & Cellular Proteomics. April 2008.
The above story is based on materials provided by American Society for Biochemistry and Molecular Biology. Note: Materials may be edited for content and length.
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