Taylor, Susan
Structure, Function, Dynamics, and Localization of PKA as a Prototype for the Protein Kinase Superfamily.

Contact Information
Professor of Chemistry and Biochemistry
Professor of Pharmacology
Howard Hughes Medical Institute

Office: Leichtag Bldg 415
Phone: 858-534-3677
Email: staylor@ucsd.edu
Web: susantaylorlab.ucsd.edu
Group: View group members
1968 Ph.D., Johns Hopkins University
1964 B.A., University of Wisconsin
Awards and Academic Honors
Vanderbilt Prize in Biomedical Sciences
FASEB Excellence in Science Award
Elected Fellow of the American Association for Advancement of Science (AAAS)
ASBMB William C. Rose Award
Garvan-Olin Medal, American Chemical Society
Howard Hughes Medical Institute Investigator
Elected into the National Academy of Sciences
Elected into Institute of Medicine
Edwin G. Krebs Lecture in Molecular Pharmacology, University of Washington, School of Medicine, Seattle
President-elect, President, past President, ASBMB
Hans Lindner Memorial Lecture, The Weizmann Institute, Rehovot, Israel
Elected into the American Academy of Arts and Sciences
Editorial Board, J. Biol. Chem
Research Interests
Our primary focus is to understand the structure, function and dynamics of cAMP-dependent protein kinase (PKA) using biochemical, biophysical and recombinant approaches. The catalytic (C) subunit was the first protein kinase structure to be solved and continues to serve as a prototype for all protein kinases, now recognized as one of the largest gene superfamilies. In parallel with crystallography, kinetics, fluorescence, H/D exchange, and small angle Xray/neutron scattering are used to define conformational changes, ligand binding sites, and sites of protein:protein interaction.

Structures of RIα and RIIβ regulatory subunits reveal critical isoform-specific differences. Most recently holoenzyme complexes were solved for RIα, RIIα, and RIIβ, and these reveal major conformational changes in the R subunits as they release cAMP and bind to the C subunit. Based on SAXS, the architecture of the holoenzymes differ significantly. The dimerization domain at the R-subunit N-terminus serves as a docking site for A Kinase Anchoring Proteins (AKAPs). Structures of the D/D domains for RIα and RIIα were solved by NMR and by crystallography, respectively.

Plasmids encoding for GFP-tagged proteins are used to probe kinase function in cells. This allows us to look at subcellular localization and translocation, and to detect PKA activity in individual living cells. We are now characterizing the structure and subcellular localization of two novel AKAPs, D-AKAP1 and D-AKAP2, that bind to both RI and RII. D-AKAP1 targets PKA to the outer mitochondrial membrane while D-AKAP2, which binds to PDZ domains and Rab 4/11, is involved in late endocytosis.

Primary Research Area
Interdisciplinary interests

Outreach Activities
Mentoring of Under Represented Students. I have always been very conscientious about recruiting and mentoring underrepresented students. As the PI on the Molecular Biophysics Training Grant, I have gone out of my way to make certain not only that we recruit underrepresented students but also that we mentor them well once they arrive.

In my own lab I often have undergraduates who come from underrepresented backgrounds and I have been very successful in placing these undergraduates in graduate programs or in professional schools upon completion of their degrees. I also have had undergraduate students who have obtained a MARCS (Minority Access to Research Careers) fellowship from the NIH which will allow them to work in a lab during the academic year and then during the summers.
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Selected Publications