Sally A Prigent

Sally Prigent Tel: +44 (0)116 229 7070

Personal details

  • PhD: University of Cambridge, 1990
  • Post-doctoral work: Imperial Cancer Research Fund (1990-1993)
  • Cancer Center, University of California, San Diego, USA (1993-1996)
  • Joined Department of Biochemistry in 1996


Signal transduction by receptor tyrosine kinases

Receptor tyrosine kinases are involved in development, normal cell growth and differentiation. These receptors are classified into groups according to their primary amino acid sequence and domain structure. In this laboratory we are particularly interested in two different families: the epidermal growth factor (EGF) receptors; and the vascular endothelial cell growth factor (VEGF) receptors, both of which are implicated in human disease.

The epidermal growth factor receptor family comprises four members, and is probably the most extensively studied group of receptors. This family has been implicated in human cancer where mutation or over-expression of one or more family members is commonly observed. Fifteen ligands have been identified which interact with different combinations of the four EGF-like receptors, either as homo- or hetero-dimers.

This complex series of interactions leads to an enormous potential for signalling diversity. We are interested in the differences in the signalling pathways initiated by different receptor/ligand combinations, particularly at the level of gene transcription.

The vascular endothelial cell growth factor (VEGF) receptors are less well characterised than the EGF receptors and have a different biological role. They are required for the development of the vasculature in embryos; in adults are mainly responsible for promoting vascular permeability, their mitogenic properties being limited to wound healing, and such disease states as cancer, diabetic retinopathy and atherosclerosis.

Since these receptors play such a central role both in development and disease, it is important to understand the molecular mechanism by which they signal. This knowledge may facilitate the rational design of inhibitors which could uncouple the ligand-binding event from a specific downstream effector pathway.

To this end, we have used the yeast two-hybrid system to identify novel proteins which interact with the intracellular portion of Flt1 and KDR. We are currently investigating the role of two novel proteins identified, in addition to assessing the role of known signalling pathways in endothelial cell function. A wide variety of molecular biology techniques are being used for DNA manipulation and RNA isolation, in addition to procedures for protein purification and analysis, and functional assessment of protein-protein interaction by the yeast two-hybrid system.


  1. Prigent SA, Gullick WJ. (1994) Identification of c-erbB-3 Binding-Sites for Phosphatidylinositol 3'-kinase and Shc using an EGF Receptor c-erbB-3 Chimera EMBO J. 13, 2831-2841
  2. Prigent SA, Pillay TS, Ravichandran KS, Gullick WJ. (1995) Binding of Shc to the NPXY Motif is Mediated by its N-Terminal Domain. J. Biol. Chem. 270, 22097-22100
  3. Prigent SA, Nagane M, Lin H, Huvar I, Boss GR, Feramisco JR, Cavenee WK, Su Huang H-J. (1996) Enhanced Tumorigenic Behavior of Glioblastoma Cells Expressing a Truncated EGF Receptor is Mediated Through the Ras-Shc-Grb2 Pathway. J. Biol. Chem. 271, 25639-25645

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