biochemistry of cell communication: proprioception (Introduction)

by David Turell , Monday, November 28, 2016, 19:53 (2703 days ago) @ David Turell

A large portion of the chemical roles is explained:

http://medicalxpress.com/news/2016-11-protein-enables-brains-muscles.html

"A huge colony of receptors must be optimally positioned and functioning on our muscle cells for our brains to talk with our bodies so we can walk and breathe.

"Now scientists have found that a protein believed to help anchor that city of receptors also helps ensure their formation and function and slow their degradation.

***

"The protein is rapsyn, and the receptors are for acetylcholine, a neurotransmitter that motor neurons release to activate our muscle cells. Rapsyn is made by our muscle cells and considered a sort of biological anchor that interacts with the acetylcholine receptors to ensure that they are optimally positioned for our muscles to receive orders from our brain.

"'For precise, efficient synapse function, the receptors have to be extremely highly concentrated at exactly the right place," Mei said.

"The connection, or synapse, the cells form is called the neuromuscular juncture. During development, neurons in the spinal cord reach out to muscle cells to form this direct line of communication. To make that connection, neurons release the protein agrin, which reaches out to LRP4, a protein on the muscle cell surface. This activates MuSK, an enzyme that supports the clustering of receptors on the muscle cell surface that will enable communication.

"Now Mei and his collaborators have shown that rapsyn does not just help hold these receptors in place on the muscle cell, but also functions as an enzyme to help drive the formation of the neuromuscular juncture through a process called neddylation. In fact, agrin and MuSK also aid this neddylation.

"The newly discovered action occurs in one of three domains, or parts, of rapsyn called RING, whose specific function was previously unknown. Rapsyn's classic scaffolding function is in another portion; a third portion has a still unknown role.

"The RING finding is a bit of a surprise since in biology anchor proteins like rapsyn typically don't have this enzymatic activity. "This anchor is active," Mei said. In fact, this is the synapse brain protein found that appears to have both these essential jobs with receptors.

"It was known that there's a lot of rapsyn near the acetylcholine receptors at the neuromuscular juncture and there is fairly constant turnover of both. The new finding indicates that rapsyn helps ensure plenty of receptors are always present in this dynamic environ.

***

"They still have plenty of questions, like if rapsyn also changes the function of the receptors, as Mei suspects. They also want to see if mutations in these other parts of rapsyn impact the enzymatic role of the RING domain, since there is evidence that mutations in other portions also can lead to deadly breathing problems. The scientists also are pursuing the function of the third rapsyn portion.

"And that's only the tip of the iceberg and a clue, Mei theorizes, to also take a look at anchor proteins throughout the body, including the brain itself. He is already looking at classic anchoring proteins, such as PSD-95, in the neuron-to-neuron connections, for any evidence of enzymatic activity - and potential new therapeutic targets - there."

Comment: More and more complexity is discovered as research progresses. Rapsyn acts as an attractor and an enzyme at the same time. How did that evolve? Not stepwise. Again highly suggestive of saltation by God.