Updated: Mar 15
Don't miss our webinar featuring Dr. Margaret Stratton (UMass Amherst), talking about her work on the role of #CaMKII in different tissues. Mass photometry has been used to quantitatively determine the stoichiometry of different variants of this crucial oligomeric enzyme.
Ca2+-calmodulin dependent protein kinase II (CaMKII) is a crucial oligomeric enzyme in neuronal and cardiac signaling, fertilization and immunity. Our work is focused on understanding the role of this fascinating enzyme in different tissues. We have used RNA sequencing to determine which transcripts are present in human hippocampus and we are characterizing these different variants in terms of their activation profiles. From these studies, we have found that the hub domain also plays a regulatory role, and structural studies (SAXS and cryoEM) indicate this is likely through interactions between the kinase and the hub domains. CaMKII is known to adopt varying stoichiometries, and we are using Mass Photometry to quantitatively determine the predominant stoichiometry of each variant. Additionally, we use a dilution series to estimate the dissociation constant for different variants. Taken together, we hope that by gaining an understanding of CaMKII in vitro and in cells, we will be able to better understand medical conditions in which CaMKII is implicated, such as memory deficiencies and infertility.
Margaret Stratton has been an assistant professor at the University of Massachusetts Amherst since 2015. Prior to this, she was a Jane Coffin Childs Fellow at UC Berkeley, where she completed her postdoctoral research focused on understanding CaMKII subunit exchange under the supervision of Prof. John Kuriyan. She also has a PhD in Biochemistry and Molecular Biology from SUNY Upstate, where she worked as a PI for Prof. Stewart Loh, focused on protein folding and designing protein sensors, as well as a Bachelor's degree in Biochemistry at Stonehill College.