Gillian Air  /  Sanjay Bidichandani  /  Robert Broyles
  Paul DeAngelis  /  Jay Hanas  /  Martin Levine  /  Guangpu Li 

Jialing Lin  /  Hiroyuki Matsumoto  / Blaine Mooers /  Ann Louise Olson 

Karla Rodgers  /  Robert Steinberg  /  Leon Unger  /  Paul Weigel   /  Christopher West 

Endocytosis/endosome fusion: molecular mechanism and function in signal transduction and regulation of cell growth and differentiation

Cells are basic building blocks of living organisms. Endocytosis is a fundamental cellular process for uptake of nutrients, regulation of cell surface receptors, and maintenance of cell homeostasis. While it is an important cellular function, endocytosis is often employed by microorganisms like viruses for entry and infection of cells. Our research is directed towards understanding the molecular basis of endocytosis and its role in regulation of cell growth and differentiation, which may provide valuable knowledge on how this cellular process is involved in human diseases such as cancer and infectious diseases and whether endocytosis can be targeted to develop therapeutics.  Current projects include (1) mechanism of Rab5-regulated endosome fusion, which is a critical step during  endocytosis and (2) Role of endocytosis in nerve growth factor (NGF)-mediated signal transduction and neuron differentiation. We hope to describe endocytosis/endosome fusion in molecular terms and identify regulatory mechanisms that control the activity of these cellular processes during cell growth and differentiation.

Selected Publications:

Zhu, H., Zhu, G., Liu, J., Liang, Z., Zhang, X.C., and Li, G. (2007) Rabaptin-5-independent Membrane Targeting and Rab5 Activation by Rabex-5 Mol. Biol. Cell 18:4119-4128.

Zhu, G., Chen, J., Liu, J., Brunzelle, J.S., Huang, B., Wakeham, N., Terzyan, S., Li, X., Rao, Z., Li, G., and Zhang, X.C. (2007) Structure of the APPL1 BAR-PH domain and  characterization of its interaction with Rab5. EMBO J. 26:3484-3493.

Liu, J., Lamb, D., Chou, M., Liu, Y-J., Li, G. (2007) Nerve Growth Factor-mediated Neurite Outgrowth via Regulation of Rab5. Mol. Bio. Cell 18:1375-1384.

Liang, Z. and Li, G. (2005) Recombinant Sindbis virus expressing functional GFP in the nonstructural protein nsP3. Gene Therapy & Mol. Bio. 9:317-324.

Zhu, G., Zhai, P., Liu, J., Terzyan, S., Li, G., and Zhang, X. C. (2004) Structural basis of Rab5-Rabaptin5 interaction in endocytosis. Nature Struc. & Mol. Biol. 11:975-983.

Zhu, G., Zhai, P., He, X., Wakeham, N., Rodgers, K., Li, G., Tang, J., and Zhang, X. C. (2004) Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. EMBO J. 23:3909-3917.

Li, G. and Zhang, X.C. (2004) GTP hydrolysis mechanism of Ras-like GTPases. J. Mol. Biol. 340:921-932.

Liang, Z., Veeraprame, H., Bayan, N., and Li, G. (2004) C-terminus of prenylin is important in forming a dimer conformation necessary for ER to Golgi transport. Biochem. J. 380:43-49

Terzyan, S., Zhu, G., Li, G., and Zhang, X. C. (2004) Refinement of the structure of human Rab5a GTPase domain at 1.05 Å resolution. Acta Crystallogr D Biol Crystallogr. 60:54-60.

Zhai, P., He, X., Liu, J., Wakeham, N., Zhu, G., Li, G., Tang, J., and Zhang, X. C. (2003) The interaction of the human GGA1 GAT domain with Rabaptin-5 is mediated by residues on its three-helix bundle. Biochemistry 42:13901-13908.

Li, G. and Qian, H. (2003) Sensitivity and specificity amplification in signal transduction. Cell Biochem. Biophy. 39:45-59.

Li, G., (2003) Biology can be helpful to open-minded physicists. Nature 421:111.

Li, G., (2002) GTP-binding loop. In Encyclopedia of Life Sciences. Nature Publishing Group. http://www.els.net

Li, G. and Qian, H., (2002) Kinetic timing: a novel mechanism that improves the accuracy of GTPase timers in endosome fusion and other biological processes. Traffic 3:249-255.

Lin, J., Liang, Z., Zhang, Z., and Li, G., (2001) Membrane topography and topogenesis of prenylated Rab acceptor (PRA1). J. Biol. Chem. 276:41733-41741.

Li, G. and Liang, Z., (2001) Phosphate-binding loop and Rab GTPase function: mutations at Ser29 and Ala30 of Rab5 lead to loss-of-function phenotype.  Biochemical Journal 355:681-689.

Liang, Z. and Li, G, (2000) Mouse prenylated Rab acceptor is a novel Golgi membrane protein.  Biochem.  Biophy. Res. Comm. 275: 509-516.

Liang, Z., Mather, T., and Li, G., (2000) GTPase mechanism and function: new insights from systematic mutational analysis of the phosphate-binding loop residue Ala30 of Rab5. Biochem. J. 346:501-508.

Liu, K., and Li, G., (1998) Catalytic domain of the p120 Ras GAP binds to Rab5 and stimulates its GTPase activity. J. Biol. Chem. 273:10087-10090.

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