Ryu, Sung Ho, Ph.D.

Professor
Department of Life Science
Division of Molecular and Life Sciences
Signal transduction & Proteomics

Publications Abstract
E-mail sungho@postech.ac.kr
Phone +82-54-279-2292(office)
          +82-54-279-5989(lab.)
Laboratory Signaling Proteome lab.

Profile |  Research Interests  |  Selected Publications

Profile

Research Interests

Signal Transduction
When extracellular signals, such as neurotransmitters, hormones, and growth factors, bind to their specific receptors, phospholipids breakdown is one of the immediate responses. The resulting breakdown products become second messengers to amplify the extracelluar signals, then the signals from the second messengers are transcended to various effector molecules, which, in turn, transduce their signals to next signaling mediators, and so forth. The final effects of the signal transduction would be one or more of the many cellular phenomena, such as proliferation, differentiation, or apoptosis.
The major research goals of the Signal Transduction Laboratory is the identification of the mechanism of signal transduction pathway mediated by phospholipases. Based on the substrate specificity and the produced second messengers, the phospholipases are classified to A, C, and D. Our lab has focused on the identification of the regulatory mechanisms of and the discovery of new molecular mediators for the signal transduction of phospholipase C and D. These studies include following studies. Purification of core signaling molecules such as phospholipases and its kinetic studies among various subtypes of the phospholipases; identification of binding proteins and in vitro molecular binding studies between phospholipases and their putative effectors; establishing transient and permanent cell lines expressing signal transduction-related molecules for in vivo studies. The accumulations of knowledges and experiences concerning the signal transduction pathway for the last decade allow us to expand our realm of research, not only in width but in depth, to the molecular libraries, such as synthetic peptides for the discovery of agonists or antagonists, which ultimately lead to the developments of new medicines. Recently, to provide valuable informations for the basic researchers as well as ideas for the industrial application in the field of signal transduction, we are going to characterize molecularly SMMC (signaling molecule multicomplex) which composes of signal machinery by using PMT (proteome molecular technology).

Selected Publications 

1. Kim, Y., Lee, B.D., Kim, O., Bae, Y.S., Lee, T., Suh, P.G., and Ryu, S.H. (2006). Pituitary adenylate cyclase-activating polypeptide 27 is a functional ligand for formyl peptide receptor-like 1. J Immunol 176, 2969-2975.
2. Baek, M.C., Kim, S.J., Yea, K., Kim, Y., Lee, B.D., Kim, J., Lee, H.J., Kang, M.H., Choi, S.K., Kim, J.I., et al. (2006). Ligand profiling and identification technology for searching bioactive ligands. Proteomics 6, 1741-1749.
3. Kim, J.H., Kim, H.W., Jeon, H., Suh, P.G., and Ryu, S.H. (2006). Phospholipase D1 regulates cell migration in a lipase activity-independent manner. J Biol Chem 281, 15747-15756.
4. Lee, C.S., Kim, I.S., Park, J.B., Lee, M.N., Lee, H.Y., Suh, P.G., and Ryu, S.H. (2006). The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis. Nat Cell Biol 8, 477-484.
5. Ha, S.H., Kim, D.H., Kim, I.S., Kim, J.H., Lee, M.N., Lee, H.J., Jang, S.K., Suh, P.G., and Ryu, S.H. (2006). PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals. Cell Signal 18, 2283-2291.
6. Lee, M.S., Yoo, S.A., Cho, C.S., Suh, P.G., Kim, W.U., and Ryu, S.H. (2006). Serum amyloid A binding to formyl peptide receptor-like 1 induces synovial hyperplasia and angiogenesis. J Immunol 177, 5585-5594.
7. Yea, K., Kim, J., Lim, S., Park, H.S., Park, K.S., Suh, P.G., and Ryu, S.H. (2008). Lysophosphatidic acid regulates blood glucose by stimulating myotube and adipocyte glucose uptake. J Mol Med 86, 211-220.
8. Lee, H.Y., Yea, K., Kim, J., Lee, B.D., Chae, Y.C., Kim, H.S., Lee, D.W., Kim, S.H., Cho, J.H., Jin, C.J., et al. (2008). Epidermal growth factor increases insulin secretion and lowers blood glucose in diabetic mice. J Cell Mol Med 12, 1593-1604.
9. Chae, Y.C., Kim, J.H., Kim, K.L., Kim, H.W., Lee, H.Y., Heo, W.D., Meyer, T., Suh, P.G., and Ryu, S.H. (2008). Phospholipase D activity regulates integrin-mediated cell spreading and migration by inducing GTP-Rac translocation to the plasma membrane. Mol Biol Cell 19, 3111-3123.
10. Lee, H.Y., Jung, H., Jang, I.H., Suh, P.G., and Ryu, S.H. (2008). Cdk5 phosphorylates PLD2 to mediate EGF-dependent insulin secretion. Cell Signal 20, 1787-1794.
11. Yoon, J.H., Yea, K., Kim, J., Choi, Y.S., Park, S., Lee, H., Lee, C.S., Suh, P.G., and Ryu, S.H. (2009). Comparative proteomic analysis of the insulin-induced L6 myotube secretome. Proteomics 9, 51-60.
12. Yea, K., Kim, J., Lim, S., Kwon, T., Park, H.S., Park, K.S., Suh, P.G., and Ryu, S.H. (2009). Lysophosphatidylserine regulates blood glucose by enhancing glucose transport in myotubes and adipocytes. Biochem Biophys Res Commun 378, 783-788.
13. Lee, C.S., Kim, K.L., Jang, J.H., Choi, Y.S., Suh, P.G., and Ryu, S.H. (2009). The roles of phospholipase D in EGFR signaling. Biochim Biophys Acta 1791, 862-868.
14. Lee, M.N., Ha, S.H., Kim, J., Koh, A., Lee, C.S., Kim, J.H., Jeon, H., Kim, D.H., Suh, P.G., and Ryu, S.H. (2009). Glycolytic flux signals to mTOR through glyceraldehyde-3-phosphate dehydrogenase-mediated regulation of Rheb. Mol Cell Biol 29, 3991-4001.
15. Chae, Y.C., Lee, S., Heo, K., Ha, S.H., Jung, Y., Kim, J.H., Ihara, Y., Suh, P.G., and Ryu, S.H. (2009). Collapsin response mediator protein-2 regulates neurite formation by modulating tubulin GTPase activity. Cell Signal 21, 1818-1826.
16. Lee, J.S., Kim, I.S., Kim, J.H., Cho, W., Suh, P.G., and Ryu, S.H. (2009). Determination of EGFR endocytosis kinetic by auto-regulatory association of PLD1 with mu2. PLoS One 4, e7090.
17. Yea, K., Kim, J., Yoon, J.H., Kwon, T., Kim, J.H., Lee, B.D., Lee, H.J., Lee, S.J., Kim, J.I., Lee, T.G., et al. (2009). Lysophosphatidylcholine activates adipocyte glucose uptake and lowers blood glucose levels in murine models of diabetes. J Biol Chem 284, 33833-33840.
18. Kim, J.H., Park, J.M., Yea, K., Kim, H.W., Suh, P.G., and Ryu, S.H. Phospholipase D1 mediates AMP-activated protein kinase signaling for glucose uptake. PLoS One 5, e9600.
19. Chae, Y.C., Kim, K.L., Ha, S.H., Kim, J., Suh, P.G., and Ryu, S.H. Protein kinase Cdelta-mediated phosphorylation of phospholipase D controls integrin-mediated cell spreading. Mol Cell Biol 30, 5086-5098.
20. Kim, H.W., Ha, S.H., Lee, M.N., Huston, E., Kim, D.H., Jang, S.K., Suh, P.G., Houslay, M.D., and Ryu, S.H. Cyclic AMP controls mTOR through regulation of the dynamic interaction between Rheb and phosphodiesterase 4D. Mol Cell Biol 30, 5406-5420.
21. Lee, D.W., Park, K.M., Banerjee, M., Ha, S.H., Lee, T., Suh, K., Paul, S., Jung, H., Kim, J., Selvapalam, N., et al. Supramolecular fishing for plasma membrane proteins using an ultrastable synthetic host-guest binding pair. Nat Chem 3, 154-159.
22. Jeon, H., Kwak, D., Noh, J., Lee, M.N., Lee, C.S., Suh, P.G., and Ryu, S.H. Phospholipase D2 induces stress fiber formation through mediating nucleotide exchange for RhoA. Cell Signal 23, 1320-1326.

Division of Molecular & Life Sciences| POSTECH