Author Interviews / 09.10.2019

MedicalResearch.com Interview with: Dr. Aurimas Vyšniauskas PhD Center for Physical Sciences and Technology Vilnius, Lithuania MedicalResearch.com: What is the background for this study? Response: Fluorescent viscosity sensors (also known as molecular rotors) are small molecules that emit light when excited by a laser and the lifetime of their emission is affected by viscosity around the molecule. Higher is the viscosity, longer is the duration of the emission. These molecules are especially useful for sensing viscosity in small biological objects, like a living cell. This is very tricky to do using other methods simply due to a very small size of a cell. Many scientists are interested in the viscosity inside the cell because it tells us how quickly various proteins and other molecules move and reactions in a cell occur. Knowing this information would help us to better understand how various diseases, such as diabetes or Alzheimers, change inner environment of affected cells. (more…)
Author Interviews / 02.08.2017

MedicalResearch.com Interview with: H. Eric Xu, Ph.D. Professor, Center for Cancer and Cell Biology Van Andel Research Institute  MedicalResearch.com: What is the background for this study? What are the main findings? Response: G protein–coupled receptors (GPCRs) comprise the largest family of cell surface signaling receptors and drug targets, with about 30 percent of drugs currently on the market interacting with these receptors. GPCR signaling is primarily mediated through two pathways: G proteins or arrestins, each of which drives distinct physiologic and therapeutic effects on GPCR ligands. Current GPCR drugs often activate or block both pathways, leading to therapeutic effects as well as unwanted side effects. An ideal GPCR drug will have a therapeutic effect but block the side-effects by selectively modulating either the G protein or arrestin pathway. The switch between the G protein and arrestin pathways is determined by the phosphorylation of the GPCR, the underlying mechanism of which has been a long sought-after question in the field. Our study uncovered and validated the phosphorylation pattern, which serves as the instructional code to switch on the arrestin pathway. Furthermore, the code appears to be universally applicable to the proteome of GPCRs and could serve as a guiding light for understanding other GPCR-arrestin interactions and arrestin-biased signaling. (more…)