In 1991, Taylor and her colleagues at UCSD determined the three-dimensional structure of the catalytic subunit of protein kinase A— the first crystal structure solved for any protein kinase. Even today, the structure continues to serve as a prototype for the entire protein kinase family. In subsequent years, Taylor has solved the structures of the protein’s regulatory subunits, as well as the structure of the entire multisubunit PKA complex, which provides insights into cAMP activation and PKA cooperativity.
“[Susan Taylor’s] structure of protein kinase A changed the way we think about kinases,” said Jack Dixon, a professor at the University of California, San Diego, and vice president and chief scientific officer of the Howard Hughes Medical Institute. “These enzymes have become important drug targets for cancer and other diseases, and Susan’s thoughtful insights into their structure and function have led the field for many years.”
More recently, Taylor has been addressing other PKA-related topics such as identifying its subcellular location, in collaboration with Roger Y. Tsien, and examining how the scaffold proteins DAKAP-1 and -2 bring together PKA and its substrates.
Taylor has received numerous awards for her studies, including the American Society for Biochemistry and Molecular Biology’s William C. Rose Award, the Wyeth Research Chemistry Award, the American Chemical Society’s Garvin-Olin Medal and the Institute of Electrical and Electronics Engineers’ Forefronts of Large Scale Computation Award. She was elected to the American Academy of Art and Sciences in 1992 and to both the Institute of Medicine and the National Academy of Sciences in 1997. Taylor also served as ASBMB president in 1995.
Angela Hopp (email@example.com) is managing editor for special projects at ASBMB. Nick Zagorski (firstname.lastname@example.org) is a science writer at ASBMB.