Ph.D., Assistant Professor
St. Albert Hall :
Dr. Yu, completed his doctorate at the Chinese Academy of Sciences
where he studied proteins that function in plant photosynthesis. He
then had his postdoctoral training at Columbia University, studying
Nicotinic acetylcholine receptor and transient receptor potential
(TRP) channels. Before he joined St. John's University in 2012, Dr.
Yu was an Associate Research Scientist at the Department of
Biological Sciences at Columbia University.
Ion channels are membrane proteins that
control the flow of ions across
the cell membrane. Ion channels play essential roles in a wide range of physiological processes, such
as electrical signaling in nerve and muscle, fluid and electrolyte
balance within cell, and cellular signal transduction. Ion channels
have been implicated in many human diseases and has been frequently
selected as targets for searching new drugs.
The research in our lab currently focuses on
understanding structure and function of a group of ion channels
called transient receptor potential (TRP) channels. TRP channels are
conserved through evolution and are found in most organisms,
tissues, and cell-types where they mainly sever as cellular sensors
and play critical roles in sensory physiology. TRP channels have been
shown to articipate in many biological processes, including
sensation of pain, hot and cold
temperature, tastes, vision, and osmotic and mechanical pressure. A combined molecular biology,
biochemistry, biophysics, crystallography and electrophysiology
approach is applied in our research.
Yu Y., Ulbrich
M.H., Dobbins S., Li M.-H., Zhang K. W., Isacoff E.Y. and Yang J.,
Molecular mechanism of the assembly of an acid-sensing receptor/ion
channel complex. Nature Communications.
3:1252 doi: 10.1038/ncomms2257, 2012
Li M-H, Yu Y and Yang
J. Structural biology of TRP channels. Advances in Experimental
Medicine and Biology 704: 1-23, 2011.
Zhu J*, Yu Y* (*equal contribution), Ulbrich
M H, Li M-H, Isacoff E Y, Honig B and Yang J. Structural model of
the TRPP2/PKD1 C-terminal
coiled-coil complex produced by a combined computational
and experimental approach. Proceedings
of the National Academy of Sciences of U. S. A., 108(25):10133-10138,
Yu Y, Ulbrich M H, Li M-H, Buraei Z, Chen
X-Z, Ong A C M, Tong L, Isacoff
E Y,and Yang J. Structural and molecular basis of the assembly of the TRPP2/PKD1 complex.
Proceedings of the National Academy of Sciences of U. S. A.,
Yu Y, Shi L, and Karlin A. Structural effects
binding in the open channel of the
acetylcholine receptor. Proceedings of the National Academy of
Sciences of U. S. A., 100(7): 3907-3912, 2003.