![Rendering of G protein based on alphafold prediction of Gpa1 structure. 1 credit Study reveals how yeast proteins communicate to find mates](https://oponame.com/wp-content/uploads/2022/10/How-yeast-proteins-communicate-to-find-mates.jpg)
Rendering of G protein based on alphafold prediction of Gpa1 structure. 1 credit
Understanding the family of cellular on/off switches known as G proteins is important because these proteins control much of the communication between cells in the human body and beyond. A new study from the University of Maine has revealed more details about how these essential proteins function in coordinating the cellular response to two conflicting signals in yeast, which could lead to a better understanding of the signaling processes involved. in human health.
A team of researchers led by Josh Kelley, an associate professor of biochemistry at UMaine, is studying G proteins in yeast in hopes of being able to tell us how these proteins work in humans. Human cells commonly sense the outside world and receive signals from other parts of the body through receptors that span the cell membrane called G protein-coupled receptors (GPCRs). GPCRs sense chemical signals outside the cell and activate a G protein inside the cell to initiate an internal cellular signal. Yeast uses a GPCR to detect and grow towards potential mating partners.
However, many proteins in the coupling pathway are shared with the pathway that controls cell division. This means that when the cell undergoes cell division and receives a signal from a potential partner, it must choose which pathway to use. What the cell is supposed to do is first complete cell division and then respond to the mating signal, but how this delay in response to the mating signal is mediated is not known.
“Cell division is a critical process. When division is abnormal, the cell is no longer able to function properly and in humans diseases such as cancer can occur,” says Cory Johnson, former Ph.D. student at the Graduate School of Biomedical Science and Engineering at the University of Maine who conducted the research for his thesis.
During the mating response, an enzyme known as MAP Kinase (MAPK) alters the regulator of G-protein signaling, or RGS. The RGS disables the mating lane, but the reason for the change was not known. The researchers used yeast strains with different RGS mutants to examine the effect of MAPK signaling on where RGS goes during the mating response and how signaling proteins were distributed in the cell. They discovered that the MAPK modification of the RGS controls where the RGS can be found, but also where the MAPK itself is located.
Even more surprisingly, the scientists found that phosphorylation of RGS promotes the completion of cytokinesis – the final division of cells at the end of mitosis – before pheromone-induced growth towards mating partners. They discovered that RGS interacts with a protein known to control the end of mitosis, called Kel1. RGS binding to Kel1 was found to be controlled by the MAPK modification of the RGS, finally answering the long-standing question of why this modification occurs. Failure to alter the RGS results in failure of cytokinesis, which can have catastrophic effects on the cell.
“We were surprised to see such a striking result because until now, there was no evidence that RGS was involved in the regulation of cell division,” says Johnson.
“Overall, this research is exciting because it sheds light on a potential signaling link in cells, where two incoming messages are received and cells interpret which signal has the highest priority to follow,” says co-author William Simke. of the study and former master’s student at UMaine.
“We hope our data can inform the scientific community of potential new mechanisms related to disease development,” says Johnson.
The study was published in August 2022 in the journal Life Sciences Alliance.
Short telomeres impede germ cell specification by up-regulating MAPK and TGFβ signaling
William C Simke et al, RGS phosphorylation regulates MAP kinase localization and promotes completion of cytokinesis, Life Sciences Alliance (2022). DOI: 10.26508/lsa.202101245
Provided by the University of Maine
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