Guest Speaker: Richard S. Lewis, Ph.D., Professor of Molecular and Cellular Physiology
Speaker Bio: Dr. Lewis graduated from Yale University in 1978 with a B.S. degree in Molecular Biophysics and Biochemistry and earned his Ph.D. in Neurobiology at Caltech in the lab of Dr. James Hudspeth, where his work on the ionic basis of frequency tuning in hair cells sparked a lifelong interest in the mechanisms and functions of ion channels. As a postdoctoral fellow with Dr. Michael Cahalan at UC Irvine, he discovered new varieties of K+, Cl-, and Ca2+ channels in T lymphocytes, including the Ca2+ release-activated Ca2+ (CRAC) channel. In 1990 he joined the Department of Molecular and Cellular Physiology at Stanford and served as Department Chair from 2004 to 2009, becoming Emeritus in 2026. His lab at Stanford has made important advances in understanding the biophysical properties of CRAC channels, the molecular and cellular mechanisms governing their activation, and their functions in controlling gene expression, lymphocyte motility and immune synapse organization and dynamics. In recognition of these achievements, Dr. Lewis was elected to the National Academy of Sciences (2020) and received the Cole Award from the Biophysical Society (2021).
Talk Title: "Molecules in motion: the cellular and molecular dynamics of store-operated calcium channels"
Abstract: Store-operated calcium channels, essential for maintaining calcium signals in excitable and non-excitable cells, are unique in being activated by depletion of Ca2+ from the lumen of the endoplasmic reticulum. In this lecture, I will trace the series of breakthroughs that revealed an activation mechanism in which the ER protein STIM1 detects Ca2+ depletion, clusters at ER–plasma-membrane junctions, and couples to mobile Orai1/CRAC channels to drive calcium entry across the plasma membrane. Most recently, our studies using single-molecule FRET offer new insight into the conformational changes and dynamic interactions through which STIM1, the master regulator of store-operated calcium entry, transitions from its inactive state to its Orai1-activating form.
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