Steven C. King
Steven C. King, Ph.D. (Harvard, 1990)
Dr. King's academic interests are in the
areas of biochemistry, physiology, and pharmacology. His research
has been focused on elucidating details of the biochemistry and genetics of
membrane transport proteins, generally, and particularly on determining how the
structure of a GABA transport protein determines its function. GABA
transport inhibitors facilitate GABAergic transmission and exhibit clinically
useful anticonvulsant activity. Novel GABA transport inhibitors may be
anticipated to complement the sedative and anxiolytic properties of
barbiturates and benzodiazepines, which facilitate GABAergic transmission by a
different mechanism. Dr. King pioneered the use of bacterial transport
systems to model analogous neurotransmitter transport systems from the
mammalian nervous system.
Selected PublicationsZhang W, Campbell HA, King SC, Dowhan W. Phospholipids as determinants of membrane protein topology. Phosphatidylethanolamine is required for the proper topological organization of the gamma-aminobutyric acid permease (GabP) of Escherichia coli.J Biol Chem. 2005;280(28):26032-8. Epub 2005 May 12.
King SC. The "Transport Specificity Ratio": a structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysis.BMC Biochem. 2004;5:16.
King SC, Brown-Istvan L. Use of the transport specificity ratio and cysteine-scanning mutagenesis to detect multiple substrate specificity determinants in the consensus amphipathic region of the Escherichia coli GABA (gamma-aminobutyric acid) transporter encoded by gabP. Biochem J. 2003 Dec 15;376(Pt 3):633-44.
King SC, Hu LA, Pugh A. Induction of substrate specificity shifts by placement of alanine insertions within the consensus amphipathic region of the Escherichia coli GABA (gamma-aminobutyric acid) transporter encoded by gabP. Biochem J. 2003;376(Pt 3):645-53.
Hu LA, King SC. Identification of the amine-polyamine-choline transporter superfamily 'consensus amphipathic region' as the target for inactivation of the Escherichia coli GABA transporter GabP by thiol modification reagents. Role of Cys-300 in restoring thiol sensitivity to Gabp lacking Cys. Biochem J. 1999;339 ( Pt 3):649-55.