Martha S. Cyert

Biography

Dr. Martha Cyert directs a research lab that studies Ca2+-dependent signal transduction, focusing on calcineurin, the highly conserved Ca2+/calmodulin-regulated protein phosphatase that plays critical roles in muscle, immune and neural cells. Dr. Cyert pioneered studies of yeast calcineurin, where her work elucidated conserved aspects of substrate recognition and mechanisms by which the signaling network evolves. Her studies on human calcineurin uncovered the mechanism by which immunosuppressant drugs, FK506 and cyclosporine A, inhibit this enzyme. Current research focuses on establishing the human calcineurin signaling network using both experimental and computational approaches to systematically identify calcineurin targets . Professor Cyert is also an active educator. She received the Dean’s Award for Outstanding Teaching, developed an innovative, inquiry-based, introductory laboratory course that utilizes S.cerevisiae, and a summer transition program for incoming freshman from under resourced schools. She was Senior Associate Vice Provost for Undergraduate Education from 2010-13, serves on the Education committee of the American Society for Cell Biology, and has taught in Cell Biology workshops sponsored by the ASCB in Africa. She directs an NIH-funded graduate training program in Cell and Molecular Biology and is a standing member of the TWD-A study section at NIH. Dr. Cyert is a member of the Stanford Cardiovascular and Bio-X Institutes and served on the Public Affairs Advisory Council for ASBMB. She has been awarded fellowships from the American Cancer Society, the Life Sciences Research Foundation and the Lucille P. Markey Charitable Trust, and was named by Stanford University as a Terman Fellow, a Gabilan Fellow, and as the Thomas W. and Susan B. Ford University Fellow in Undergraduate Education.

Research Interest

MAPPING THE HUMAN CALCINEURIN PHOSPHATASE SIGNALING NETWORK THROUGH GLOBAL IDENTIFICATION OF SHORT LINEAR MOTIFS THAT MEDIATE SUBSTRATE RECOGNITION. FUNCTIONAL STUDIES OF HUMAN CNAβ1 SPLICE VARIANT Calcineurin is tightly controlled by Ca2+ and calmodulin, which activate the enzyme by relieving auto-inhibition of the active site, and revealing a critical binding pocket for "LxVP" substrate motifs. We are studying regulation of a conserved splice variant of the human CNAβ gene, CNAβ1, which promotes cardiac regeneration in vivo. The CNAβ1 C-terminus contains an LxVP sequence, which we showed auto-inhibits phosphatase activity by blocking substrate engagement. CNAβ1 has distinct enzymatic properties, and is relatively independent of calmodulin. Functional studies are identifying and characterizing unique protein partners for CNAβ1 and its substrates in cardiovascular and endocrine signaling.