Inositol 1,4,5-trisphosphate receptors (IP3Rs) form a family of intracellular Ca2+ channels that integrate multiple cellular stimuli (including neurotransmitters, hormones, growth factors, odorants, and light) to release Ca2+ from intracellular stores such as the endoplasmic reticulum (ER) into the cytoplasm. IP3R channels are activated by their primary ligands, Ca2+ and IP3, and are modulated via complex interactions with numerous intracellular ligands. Due to the fundamental importance of IP3R channels in cellular Ca2+ signaling which affect many human diseases, understanding the molecular architecture of this class of integral membrane proteins is of broad interest to many different research communities. A central mechanistic question in IP3R gating is how IP3 binding in the N-terminal sequence of the channel protein is communicated to the ion conduction pore formed near the C-terminus. My aim is to get subnanometer resolution three-dimensional (3D) architecture of the full-length channel protein using single-particle electron cryomicroscopy(cryo-EM) and computational methods to reveal its biological functions in terms of its molecular architecture.
Postdoctoral Research Fellow - UTHSC, Department of Biochemistry and Molecular Biology, Advisor:Irina Serysheva, 2012-present
Ph.D. - Peking University Health Science Center, Department of Biophysics, China, Advisor:Changcheng Yin, 2007-2012
B.S. - Shandong University, Department of Nursing, China, 2002-2007