Tsung-Yu Chen, M.D., Ph.D.
Center for Neuroscience
1544 Newton Court
Davis, CA 95618
Trained as an ion channel biophysicist and physiologist, Dr. Chen has studied various ion channels for more than 2 decades using a variety of experimental approaches. He has studied voltage-gated potassium channels and cyclic nucleotide-gated ion channels critical for visual and olfactory signal transductions, and has characterized the gating and permeation mechanisms of the CLC-0 chloride channel.
Recently, his research has focused on the structure, function, and modulation of CLC-1, a CLC channel expressed in vertebrate skeletal muscles. His team has found that intracellular ATP can inhibit CLC-1 channels, and that the degree of inhibition is enhanced by a lower intracellular pH. Using mutant cycle analysis, the team has confirmed binding of ATP to CLC-1. They have also demonstrated that oxidized CLC-1 channels are not sensitive to the ATP/H+ inhibition, suggesting that oxidation can dynamically regulate the function of skeletal muscles by controlling chloride channels.
Most recently, his team has begun researching calcium-activated chloride channels that are expressed abundantly in various epithelial and neuronal tissues. They are examining functional properties of CaCC and addressing the controversial issue of modulation of CaCC by calmodulin.
Johns Hopkins University
Ph.D. 1994 (Neuroscience)
National Yang-Ming Medical School
M.D. 1986, M.S. 1988 (Physiology)
Postdoctoral Fellowship (Biophysics - Ion Channels)
Society for General Physiologists
Select Recent Publications
Yu Y., Kuan A.-S., Chen T.-Y. (2014) Calcium-calmodulin does not alter the anion permeability of the mouse TMEM16A calcium-activated chloride channel. J. Gen. Physiol. 144: 115-124.
Ni Y.-L., Kuan A.-S., Chen T.-Y. (2014) Activation and Inhibition of TMEM16A Calcium-Activated Chloride Channels. PLoS ONE 9(1): e86734. doi:10.1371/ journal.pone.0086734.
Lee T.-T., Zhang X.-D., Chuang C.-C., Chen J.-J., Chen Y.-A., Chen S.-C., Chen T.-Y., Tang C.-Y. (2013) Myotonia Congenita Mutation Enhances the Degradation of Human CLC-1 Chloride Channels. PLoS ONE 8(2): e55930.
Richman D.P., Yu Y., Lee T.-T., Tseng P.-Y., Yu W.-P., Maselli R.A., Tang C.-Y., Chen T.-Y. (2012) Dominantly-inherited myotonia congenita resulting from a mutation that increases open probability of the muscle chloride channel CLC-1. Neuromol Med 14: 328-337.
Tang C.-Y., and Chen T.-Y. (2011) Physiology and pathophysiology of CLC-1: mechanisms of a chloride channel disease, myotonia. J. of Biomedicine and Biotechnology, vol. 2011, Article ID 685328, 2011. doi:10.1155/2011/685328.
Tseng P.-Y., Yu W.-P., Liu, H.-Y., Zhang X.-D., Zou X., and Chen T.-Y. (2011) Binding of ATP to the CBS domains in the C-terminal region of CLC-1. J. Gen. Physiol. 137: 357-368.
Zhang X.-D., and Chen T.-Y. (2009) Amphiphilic blockers punch through a mutant CLC-0 pore. J. Gen. Physiol. 133: 59-68.
Zhang X.-D., Tseng P.-Y., Yu W.-P., and Chen T.-Y. (2009) Blocking pore-open mutants of CLC-0 by amphiphilic blockers. J. Gen. Physiol. 133: 43-58.
Zhang X.-D. Tseng P.-Y., and Chen T.-Y. (2008) ATP inhibition of CLC-1 is controlled by oxidation and reduction. J. Gen. Physiol. 132: 421-428.
Chen T.-Y., and Hwang, T.-C. (2008) CLC-0 and CFTR: Chloride channels evolved from transporters. Physiol. Rev. 88: 351-387.