Mirror image biomolecule helps sea squirts lose their tails
Amino acids are the building blocks of living things and typically occur in a configuration known as the L-form. However, there are some exceptional examples of the structural mirror image of the L-form (known as the D-form) found in animals. D-serine is a representative D-form amino acid and plays an important role in mammals, but its role in non-mammals is unclear. Japanese researchers recently discovered a functional role for D-serine in marine invertebrates, which may provide insights into the evolution and function of D-amino acids in living organisms.
In a study published this month in Scientists’ progressA team led by the University of Tsukuba found that D-serine acts as a chemical signal that enables tissue migration in sea vapor when they lose their tails as tadpoles transform into their mature form. Their findings provide a broader understanding of the chemical signals that occur during an organism’s transformation.
In mammals, D-serine binds to an ion channel found in neurons called . notGlutamate-like D-Aspartate (NMDAR) receptors to regulate the transmission of messages in the brain. D-serine also plays a functional role in mammalian skin tissues. However, its role in non-mammals is poorly understood, which is what researchers at the University of Tsukuba have sought to solve.
“D-serine has been detected in organisms such as insects, nematodes and mollusks,” says lead author of the study, Professor Yasunori Sasakura. “Its presence worldwide in metazoans reflects the conserved presence of the protein that converts L-serine into the D form, called serine racemase.”
The team’s previous findings indicated the involvement of the serine race base in the regression of the tail of sea squirt tadpoles Siona. In this study, they sought to clarify the role of D-serine in this process and found that D-serine is responsible for the formation of a pocket in Siona The cuticle that allows the tail to bounce back into the main body. This pocket was formed by D-serine binding to NMDAR in the epidermis, causing the release of fluid-filled vesicles.
“The results were amazing,” says Professor Sasakura. We found that the release of epidermal vesicles in Siona Very similar to a process occurring in the skin of mammals, involving cation-mediated outflow. »
To assess what happened when you missed D-serine Siona Going down the tail, the research team created a mutation that abolished the protein responsible for making D-serine from L-serine. Siona Organisms lacking this protein fail to complete the tail regression, while normal organisms Siona The organizations were able to implement the process.
“Our results provide insight into how skin homeostasis is maintained in animals, contributing to further evolutionary insights into the function of D-amino acids in metazoans,” says Sasakura.
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