Racism is a pervasive and persistent problem in and out of STEM. Dr. Kohout unequivocally condemns racism and stands together with all Black, Indigenous and People of Color (BIPOC), on and off campus. She is committed to creating a diverse environment and making her lab and her teaching safe, free and welcoming to all. She welcomes people from a wide variety of backgrounds, not just because it is the right thing to do but because it makes our science, our teaching and our community stronger. She celebrates the diverse community different individuals cultivate and strives to create a space where all can develop to their full potential, bringing their full selves to the laboratory and classroom. 

Dr. Kohout views cells and their critical communication from a molecular point of view. After earning her BS in Organic Chemistry from the California Institute of Technology, she branched out to study how proteins interact with calcium and with the lipid membrane, earning a PhD in Chemistry and Biochemistry with a certificate in Biophysics from the University of Colorado, Boulder. Following her developing love of cell communication, she started her postdoctoral research at the University of California, Berkeley where she studied biophysics and neuroscience, discovering how electrical signaling is as fundamental as chemical signaling in cells. After her postdoc, Dr. Kohout started her own laboratory at Montana State University where she continued her research into neuroscience and the electrical signaling of cells while expanding to include cell biology and physiology. She recently joined the Biomedical Science faculty at Cooper Medical School of Rowan University where she will take advantage of the medical school to expand her research into more medically relevant directions. 

Research interests: Voltage dependent cell signaling

Signaling cascades are the basis for cell life. From single cells to multi-cell organisms, cells must respond to and communicate with their local environment. The higher the organism the more complicated that communication becomes with interconnected and interdependent signaling pathways. Failures in these communication pathways often lead to diseases when the cells can no longer compensate.

One of the most important sites of cell signaling is the plasma membrane, where signals from the external environment are detected, physiological and biochemical signals of the cell initiated and through which ions, water, metabolites and proteins are selectively transported. These processes involve dozens of signaling pathways, and are critical in diverse cellular processes, including setting up and discharging the membrane potential, transforming cell morphology and migration, driving cell division and differentiation. One of the key links to the regulation of these diverse phenomena is phosphatidylinositol signaling. Classically, control of this pathway has been attributed to soluble kinases and phosphatases that inter-convert phosphatidylinositol phosphates (PIPs) between forms that bind to distinct effectors. Since these effectors include ion channels and transporters, some of the fastest effects of PIP signaling are changes in membrane potential. Our research focuses on a unique membrane protein that operates in the reverse direction: responding to changes in voltage to alter PIP levels. This protein, the voltage sensing phosphatase (VSP), provides a fascinating feedback loop whose biophysical properties and physiological outcomes have yet to be determined.

VSP belongs to a specialized family of voltage sensitive proteins that allow cells to transduce changes in membrane potential into chemical signals. Basic cellular processes, such as neuronal firing and muscle contraction, rely on these voltage dependent events. Voltage sensitive proteins respond to the changes in membrane potential via a voltage-sensing domain (VSD). The most common members of this family, the voltage-gated ion channels, use the VSD to open and close a pore domain, which allows for the passive movement of ions down their concentration gradients. Instead of a pore, VSP has a phosphatase domain that dephosphorylates phosphates from PIP lipids. The phosphatase domain from VSP is quite similar to the tumor suppressor, PTEN, sharing 44% identity between the two catalytic domains.

For more information about Dr. Kohout and her research lab, please visit the lab website!

If you are interested in a position in the lab, please feel free to reach out (kohout@rowan.edu)!