Susan S. Taylor | |
---|---|
Born | 1942 (age 80–81) |
Education | University of Wisconsin, Johns Hopkins University |
Known for | Studies of protein kinase A, including the first kinase crystal structure |
Awards | |
Scientific career | |
Fields | Biochemistry |
Institutions | University of California, San Diego |
Susan Taylor (born 1942 [1] ) is an American biochemist who is a Professor of Chemistry and Biochemistry and a Professor of Pharmacology at the University of California, San Diego. She is known for her research on protein kinases, particularly protein kinase A. [2] She was elected to the Institute of Medicine and the United States National Academy of Sciences in 1996. [3] [4]
Taylor was born in 1942 in Racine, Wisconsin. [1] She attended the University of Wisconsin as an undergraduate and received a B.A. in biochemistry in 1964. Despite originally planning for a career as a medical doctor, she received her PhD in physiological chemistry from Johns Hopkins University in 1968 and then worked as a postdoctoral fellow at the Medical Research Council Laboratory of Molecular Biology in Cambridge, England, where she has said she settled on a career in research science. [5] After returning to the United States, she worked as a postdoc at the University of California, San Diego. [1] [2]
After a brief postdoc position at UCSD, Taylor joined the faculty there in the Department of Chemistry and Biochemistry in 1972 and became a full professor in 1985. [1] She was a Howard Hughes Medical Institute Investigator from 1997 to 2014. [6]
Taylor served on the editorial board of the Journal of Biological Chemistry from 1985-1990 and served a term as the president of the American Society for Biochemistry and Molecular Biology in 1995. [2]
Taylor's research group has focused on the structure and function of protein kinases, particularly protein kinase A, since shortly after she began her independent research career. [1] Her group, collaborating with Janusz Sowadski, was the first to solve the crystal structure of a protein kinase when they reported the structure of PKA in 1991. [7] The group has subsequently published a number of papers on the dynamics and mechanism of PKA, or cyclic AMP-dependent protein kinase. [8] [9] [10]
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase. PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase.
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The catalytic subunit α of protein kinase A is a key regulatory enzyme that in humans is encoded by the PRKACA gene. This enzyme is responsible for phosphorylating other proteins and substrates, changing their activity. Protein kinase A catalytic subunit is a member of the AGC kinase family, and contributes to the control of cellular processes that include glucose metabolism, cell division, and contextual memory. PKA Cα is part of a larger protein complex that is responsible for controlling when and where proteins are phosphorylated. Defective regulation of PKA holoenzyme activity has been linked to the progression of cardiovascular disease, certain endocrine disorders and cancers.
Harry F. Noller is an American biochemist, and since 1992 the director of the University of California, Santa Cruz's Center for the Molecular Biology of RNA. He has made significant contributions to our understanding of the ribosome and is a member of the National Academy of Sciences.
BIM-1 and the related compounds BIM-2, BIM-3, and BIM-8 are bisindolylmaleimide-based protein kinase C (PKC) inhibitors. These inhibitors also inhibit PDK1 explaining the higher inhibitory potential of LY33331 compared to the other BIM compounds a bisindolylmaleimide inhibitor toward PDK1.
Balanol is a fungal metabolite produced by the fungus Verticillium balanoides. It is a potent inhibitor of the serine/threonine kinases protein kinase A (PKA) and protein kinase C (PKC), binding in a similar manner with that of ATP. Balanol was discovered in 1993 in the search for novel inhibitors of PKC, a member of a family of serine/threonine kinases whose overactivation is associated with numerous human diseases of signal transduction including cancer. However, much of the research on balanol focuses on how chemical modifications of the molecular structure affect binding to PKA. Indeed, balanol, its chemically altered analogs, and their interactions with PKA in particular are used to illuminate the roles of selectivity and protein flexibility in the inhibition of kinases. For instance, the X-ray crystal structure of balanol in complex with PKA was used in order to confer selectivity and to improve pharmacological efficacy of inhibitors of the H. sapiens Akt (PKB), another serine/threonine protein kinase implicated in the proper functioning of many cellular processes.
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