Dr Lazaros Foukas


Personal Profile

Name: Lazaros Foukas Email: l.foukas@ucl.ac.uk
Title: Dr Tel:
Department: Genetics, Evolution & Environment Fax:
Position: Lecturer Address: , , London,
Research Domain: Cancer, Personalised Medicine, Populations & Lifelong Health Web Page: Personal Web Page


Research Description

Ageing is a process of gradual decline in the physiological functions of the organism. Amongst other derangements, ageing is associated with dysfunction in carbohydrate and lipid homeostatic regulatory mechanisms. Consequently, middle-aged and old individuals have a higher risk of suffering from metabolic disorders. The rapidly increasing incidence of obesity and type-2 diabetes necessitates the development of novel therapeutic agents to combat these conditions and their numerous debilitating complications.

Cell signalling pathways have been successfully targeted in the therapy of major diseases, such as cancer and inflammation. Signalling pathways that sense nutrient availability and regulate metabolic responses represent potential points of intervention for treatment of metabolic disorders. Key signalling pathways in metabolic regulation are the PI 3-Kinase (PI3K) and Target of Rapamycin (TOR) pathways.

We aim to study the mechanisms by which growth factor and nutrient sensing signalling pathways regulate metabolism and the impact of their perturbation on health in the context of ageing. We use a combination of mammalian genetics, cell based models and pharmacological approaches to identify components of cell signalling pathways which can be targeted in prevention or therapy of age-related diseases.

Research Activities

Cell signalling

age-related disease



metabolic regulation


type-2 diabetes

Education Description

UCL Collaborators

Prof Dame Linda Partridge; Prof David Gems; Dr Eugene Schuster; Dr Brian King; Prof Mika Kivimaki; Dr Daniel Pearce; Prof Meena Kumari; Prof Michael Duchen; Dr Hynek Pikhart; Dr Sally Dawson; Dr Babis Rallis

External Collaborators



    • Foukas LC, Bilanges B, Bettedi L, Pearce W, Ali K, Sancho S, Withers DJ, Vanhaesebroeck B (2013). Long-term p110α PI3K inactivation exerts a beneficial effect on metabolism.. EMBO Mol Med, 5(4), 563 - 571. doi:10.1002/emmm.201201953


    • Dubois E, Jacoby M, Blockmans M, Pernot E, Schiffmann SN, Foukas LC, Henquin JC, Vanhaesebroeck B, Erneux C, Schurmans S (2012). Developmental defects and rescue from glucose intolerance of a catalytically-inactive novel Ship2 mutant mouse.. Cell Signal, 24(11), 1971 - 1980. doi:10.1016/j.cellsig.2012.06.012


    • Foukas LC, Withers DJ (2010). Phosphoinositide signalling pathways in metabolic regulation.. Curr Top Microbiol Immunol, 346, 115 - 141. doi:10.1007/82_2010_59
    • Foukas LC, Berenjeno IM, Gray A, Khwaja A, Vanhaesebroeck B (2010). Activity of any class IA PI3K isoform can sustain cell proliferation and survival. Proc Natl Acad Sci U S A, , - . doi:10.1073/pnas.0906461107


    • Graupera M, Guillermet-Guibert J, Foukas LC, Phng LK, Cain RJ, Salpekar A, Pearce W, Meek S, Millan J, Cutillas PR, Smith AJ, Ridley AJ, Ruhrberg C, Gerhardt H, Vanhaesebroeck B (2008). Angiogenesis selectively requires the p110alpha isoform of PI3K to control endothelial cell migration. Nature, 453(7195), 662 - 666. doi:10.1038/nature06892


    • Foukas LC, Claret M, Pearce W, Okkenhaug K, Meek S, Peskett E, Sancho S, Smith AJ, Withers DJ, Vanhaesebroeck B (2006). Critical role for the p110alpha phosphoinositide-3-OH kinase in growth and metabolic regulation.. Nature, 441(7091), 366 - 370. doi:10.1038/nature04694


    • Vanhaesebroeck B, Ali K, Bilancio A, Geering B, Foukas LC (2005). Signalling by PI3K isoforms: insights from gene-targeted mice.. Trends Biochem Sci, 30(4), 194 - 204. doi:10.1016/j.tibs.2005.02.008


    • Foukas LC, Beeton CA, Jensen J, Phillips WA, Shepherd PR (2004). Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo.. Mol Cell Biol, 24(3), 966 - 975.
    • Foukas LC, Panayotou G, Shepherd PR (2004). Direct interaction of major histocompatibility complex class II-derived peptides with class Ia phosphoinositide 3-kinase results in dose-dependent stimulatory effects.. J Biol Chem, 279(9), 7505 - 7511. doi:10.1074/jbc.M303999200
    • Foukas LC, Shepherd PR (2004). Phosphoinositide 3-kinase: the protein kinase that time forgot.. Biochem Soc Trans, 32(Pt 2), 330 - 331.
    • Foukas LC, Shepherd PR (2004). eIF4E binding protein 1 and H-Ras are novel substrates for the protein kinase activity of class-I phosphoinositide 3-kinase.. Biochem Biophys Res Commun, 319(2), 541 - 549. doi:10.1016/j.bbrc.2004.04.191


    • Foukas LC, Okkenhaug K (2003). Gene-targeting reveals physiological roles and complex regulation of the phosphoinositide 3-kinases.. Arch Biochem Biophys, 414(1), 13 - 18.


    • Foukas LC, Daniele N, Ktori C, Anderson KE, Jensen J, Shepherd PR (2002). Direct effects of caffeine and theophylline on p110 delta and other phosphoinositide 3-kinases. Differential effects on lipid kinase and protein kinase activities.. J Biol Chem, 277(40), 37124 - 37130. doi:10.1074/jbc.M202101200


    • Foukas L, Heesom K, Denton R, Shepherd PR (2001). 4E-BP1 is a novel protein substrate for PI 3-kinase. FASEB J, 15(5), A902 - A902.
    • Shepherd PR, Brown RA, Chilton K, Foukas L (2001). Class-II phosphoinositide 3-kinases: A new mechanism for PI 3-kinase participation in growth factor and cytokine signalling. FASEB J, 15(4), A387 - A387.


    • Beeton CA, Chance EM, Foukas LC, Shepherd PR (2000). Comparison of the kinetic properties of the lipid- and protein-kinase activities of the p110alpha and p110beta catalytic subunits of class-Ia phosphoinositide 3-kinases.. Biochem J, 350 Pt 2, 353 - 359.


    • Foukas LC, Katsoulas HL, Paraskevopoulou N, Metheniti A, Lambropoulou M, Marmaras VJ (1998). Phagocytosis of Escherichia coli by insect hemocytes requires both activation of the Ras/mitogen-activated protein kinase signal transduction pathway for attachment and beta3 integrin for internalization.. J Biol Chem, 273(24), 14813 - 14818.


    • Charalambidis ND, Foukas LC, Zervas CG, Marmaras VJ (1996). Hemocyte surface phenoloxidase (PO) and immune response to lipopolysaccharide (LPS) in Ceratitis capitata.. Insect Biochem Mol Biol, 26(8-9), 867 - 874.
    • Charalambidis ND, Foukas LC, Marmaras VJ (1996). Covalent association of lipopolysaccharide at the hemocyte surface of insects is an initial step for its internalization--Protein-tyrosine phosphorylation requirement.. Eur J Biochem, 236(1), 200 - 206.