PHARMACOLOGY FACULTY
Selected Publications
  • (Publications before 1997 were under the name of Dong, Q.)
  • Li, J., Mao, X., Dong, L.Q., Liu, F., and Tong, L. (2007) Crystal structure of the BAR-PH and PTB domain of human APPL1. Structure, 15:525-33.
  • Wang, C., Mao, X., Wang, L., Liu, M., Wetzel, M., Guan, K-L., Dong, L.Q., and Liu, F. (2007) Crosstalk between adiponectin and insulin signaling pathways: A molecular mechanism for adiponectin as an insulin sensitizer. J. Biol. Chem. 282:7991-7996.
  • Riojas, R.A., Kikani, C.K., Wang, C., Mao, X., Zhou, L., Langlais, P.R., Hu, D., Roberts, J.L., Dong, L.Q., and Liu, F. (2006). Fine-tuning PDK1 activity by phosphorylation at Ser163. J. Biol. Chem. 281:21588-21593.
  • Mao, X., Kikani, C.K., Riojas, R.A., Langlais, P., Wang, L., Ramos, F.J., Fang, Q., Christ-Roberts, C.Y., Hong, J.Y., Kim, R.Y., Liu, F., and Dong, L.Q. (2006). APPL1 bonds to adiponectin receptors and mediates adiponectin signaling and function. Nat. Cell Biology, 8:516-523. (Highlighted article on cover page.)
  • Ramos, F.J., Langlais, P.R., Hu, D., Dong, L.Q., Liu, F. (2006) Grb10 mediates insulin-stimulated degradation of the insulin receptor: A mechanism of negative regulation. Am J Physiol Endocrinol Metab., 290:E1262-E1266.
  • Luo, M., Reyna, S.M., Wang, L., Yi, Z.P., Carroll, C.A., Dong, L.Q., Langlais, P., Weintraub, S.T., and Mandarino, L.J. (2005) Identification of IRS-1 Serine/Threonine Phosphorylation Sites Using Mass Spectrometry Analysis: Regulatory Role of Serine 1223. Endocrinology, 146:4410-4416.
  • Langlais, P., Wang, C., Dong, L.Q., Carroll, C.A., Weintraub, S.T., and Liu, F. (2005) Phosphorylation of Grb10 by Mitogen-Activated Protein Kinase: Identification of Ser150 and Ser476 of human Grb10zeta as Major Phosphorylation Sites. Biochemistry, 44:8890-8897.
  • Lim, M.A., Moon, S.Y., Zheng, Y., Wu, H., Dong, L.Q., and Liu, F. (2004) Roles of PDK-1 and PKN in regulating cell migration and cortical actin formation of PTEN-deficient cells. Oncogene, 23:9348-9358.
  • Langlais, P., Dong, L. Q., Ramos, F. J., Hu, D., Li, Y., Quon, M. J., and Liu, F. (2004). Negative regulation of insulin-stimulated MAP kinase signaling by Grb10. Mol. Endo, 18:350-358.
  • Lim, M. A., Kikani, C. K., Wick, M. J., and Dong, L. Q. (2003). Nuclear translocation of 3’-phosphoinositide-dependent kinase-1: a potential regulatory mechanism for PDK-1 function. Proc. Natl. Acad. Sci. USA. 100:14006-14011.
Lily Q. Dong
 

Lily Q. Dong

Associate Professor of Cellular & Structural Biology and Pharmacology
Ph.D., Iowa State University

Office: 210-567-4849
Email: dongq@uthscsa.edu

 

Keywords

KEYWORDS

 

Research Summary

Insulin resistance is a primary contributing factor in the pathogenesis of type 2 diabetes. This condition is characterized by the loss of insulin sensitivity in tissue, resulting in an impairment of glucose breakdown in cells, an unregulated production of glucose in hepatic cells, and a reduction of glucose uptake in skeletal muscle, resulting in a greatly increased glucose level in the bloodstream. Recently a new hormone has been identified in the human body known as adiponectin. This hormone is secreted by adipose tissue and is released into the bloodstream. The serum concentration of adiponectin is significantly reduced in type 2 diabetic and obese patients. A number of studies have shown that adiponectin is an insulin sensitizer by enhancing insulin sensitivity, which has the potential to be used therapeutically in the treatment of type 2 diabetes and obesity. However, the molecular mechanism governing adiponectin action is largely unknown.

 

Our current research interest is focused on 1) the elucidation of the molecular pathway(s) mediating adiponectin signaling in cells, 2) the investigation of the molecular mechanism regulating adiponectin levels in the human body, and 3) the molecular mechanism of the cross-talk between Insulin signaling pathway and Adiponectin signaling pathway. We have found that APPL1, an adaptor protein with multiple function domains, is a signaling molecule immediate binding to adiponectin receptors, and positively mediate adiponectin signaling in muscle cells (Mao et al., 2006, Nat. Cell Biol., 8:516-523). The findings from our studies will provice potential mechanisms behind insulin resistance and the development of type 2 diabetes.