Gachon University Cancer and Diabetes institute

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Research Outline

Insulin Signaling and Insulin Resistance
The biological versatility of phosphoinosidies (PtdIns) derivers from its unique ablity to be reversibly phosporylated at three distinct positions of the inositol headgroup. Single or combinatorial phosphorylation of the 3,4, and 5 positions on the inositol ring of PtdIns can generate several unique PtdIns, which have diverse roles in receptor-mediated signal transduction. Lipid kinases, phosphatases and lipases that produce and degrade these signaling lipids spatially and temporally control the biological activity of phosphoinositides.

Phosphoinositides signaling and their interacting proteins
Insulin controls glucose uptake through tyrosine phosphorylation of insulin receptor(IRSs)Proteins. Activation of PI3K and generation of PtdIns (3,4,5)P3 activates Akt, which, in turn, supports recyling of the glucose transporter (GLUT4). Both inhibitor of NF-kB kinase (IKKß)and JNK desensitize insulin reponsiveness through inhibitory serine phosphorylation of IRS.

Research Contents

About LAB

The long-term goal of our research is to combine structural and biochemical studies to understand the molecular mechanisms of insulin resistance, focusing on insulin receptor and insulin receptor substrates implicated in human metabolic disease. Over the next several years, we will continue to explore structure-function relationships in proteins of phosphoinositides signaling and membrane recognition domains, with particular emphasis on members of phospholipids-binding domains, phosphoinositides phosphatases, and inositol phosphate phosphatases.

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