Our brains are full of chemical heroes who make sure the electrical signals don't get out of control.
A new mouse study shows the function of a pair of proteins that are vital to maintaining this balance, which could help us better understand a range of neurological disorders.
The Rab3-Interacting molecule 1 and the serine arginine protein kinase 2 work together to modify the transmission of information between the nerves.
Without their efficient policing of neural activity, messages could either get lost due to insufficient signal, or flood important junctions, overwhelming key networks, and burying important signals in a noise.
Researchers from Germany and Australia have described in detail the chemical interplay between the two proteins in lab mice, which could one day provide therapeutic targets for conditions where this process goes awry.
Commuters might be thought of as transport terminals that connect them to different services. Some services leave the moment a few passengers arrive, while others wait until they are hit with a surge of commuters.
Guidance on when to wait and when to board is needed by this flow of travelers. Which is where the first one comes in.
Instead of waiting at the station, neurons have tiny bubbles filled with transmitters on the verge of release at the synapse, ready to spill out the moment a suitable signal arrives.
The amount of neurotransmitter released by the presynapse and the extent to which the postsynapse responds to it are strictly regulated in the brain.
Most of what we know about this regulation is based on simple organisms. Researchers noticed the activity of RIM1 when they studied the fruit flies.
It is likely that more complex animals have different mechanisms that help fine-tune their own brains, so researchers analyzed the mechanisms of the protein that was taken from mouse brains to see how it worked.
They found that the activity of neurotransmitter bubbles in the brain can be increased or decreased by adding a molecule with a group ofphosphates onto specific links of the amino-acid structure.
Johannes Alexander Müller is a neurophysiologist at University Hospital Bonn.
There is room for a range of other enzymes to be at work, further fine- tuning the process, because what happens to the phosphorylatedRIM1 proteins after they have done their job isn't clear.
It can be just as useful to know what will happen when things don't go according to plan. There are genetic clues that suggest thatRIM1 could be involved in some conditions.
McGovern wants to further clarify these relationships.
Maybe new therapeutic options for these diseases will emerge from our findings in the long term, although there is certainly a long way to go before that happens.
Cell published this research.
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