Jonathan WHITTAKER, M.R.C.P. (UK)
University College, 1973
- Director: PhD in Nutrition program (link)
- PUBLICATIONS (via PubMed)
Molecular basis of insulin binding and receptor activation.
Jonathan Whittaker obtained his MD degree at University College School of Medicine, London, England in 1971. He completed residency training in internal medicine at the University of Southampton and specialty training in Endocrinology at the University of Newcastle. He then went to the Diabetes Branch at the National Institutes of Health as a Fogarty International research Fellow in 1981. In 1984 he moved to the laboratory of Dr. Donald Steiner at the Howard Hughes Medical Institute at the University of Chicago. In 1989 he became an Assistant Professor in the Department of Medicine at the State University of New York at Stony Brook, N.Y.
In 1997 he joined the Department of Cell Signaling at the Hagedorn Research Institute in Denmark and became the Director of the Receptor Biology Laboratory at the institute in 2001. In 2002, he joined the Department of Nutrition at Case as an Associate Professor.
The major research interests of my laboratory are in the structure and function of the insulin receptor family of receptors and their cognate peptide ligands. This receptor family has long been known to be the major signaling system involved in the regulation of partitioning of nutrients and in the regulation of cellular growth in higher vertebrates. More recently, genetic studies in both vertebrates and invertebrates have implicated this receptor family in the regulation of longevity, the regulation of reproductive function and in the regulation of sex determination.
Ongoing studies in the laboratory are directed towards dissecting the molecular basis of the interaction of the receptors of this family with their cognate ligands. We have been using systematic mutational analysis to characterize the functional epitopes of both ligands and receptors. We are developing methods to over-express sub-domains of the receptors in sufficient quantity to facilitate the application of biophysical studies to the elucidation of their structure and function. We also plan to evaluate the effects
Chakravarty A, Hinrichsen J, Whittaker L, Whittaker J. Rescue of ligand binding of a mutant IGF-I receptor by complementation. Biochem Biophys Res Commun. 2005 May 27; 331(1): 74-7.
Whittaker L, Whittaker J. Rescue Characterization of the functional insulin binding epitopes of the full length insulin receptor. J Biol Chem. 2005 Mar 30; [Epub ahead of print]
Lesueur F, Cebrian A, Cranston A, Leyland J, Faid T, Clements M, Robledo M, Whittaker J, Ponder B. Germline homozygous mutations at codon 804 in the RET proto-oncogene in MTC/MEN2A patients. J Clin Endocrinol Metab. 2005 Mar 1; [Epub ahead of print]
Huang K, Xu B, Hu SQ, Chu YC, Hua QX, Qu Y, Li B, Wang S, Wang RY, Nakagawa SH, Theede AM, Whittaker J, De Meyts P, Katsoyannis PG, Weiss MA. How insulin binds: the B-chain alpha-helix contacts the L1 beta-helix of the insulin receptor. J Mol Biol. 2004 Aug 6; 341(2):529-50.
Xu B, Hu SQ, Chu YC, Huang K, Nakagawa SH, Whittaker J, Katsoyannis PG, Weiss MA. Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor. Biochemistry. 2004 Jul 6;43(26):8356-72.
Sorensen H, Whittaker L, Hinrichsen J, Groth A, Whittaker J. Mapping of the insulin-like growth factor II binding site of the Type I insulin-like growth factor receptor by alanine scanning mutagenesis. FEBS Lett. 2004 May 7;565(1-3):19-22.
Sadler L, Saftlas A, Wang W, Exeter M, Whittaker J, McCowan L. Treatment for cervical intraepithelial neoplasia and risk of preterm delivery. JAMA. 2004 May 5;291(17):2100-6.