faculty & research

 

ARTHUR KARLIN

ARTHUR KARLIN ARTHUR KARLIN

Email: ak12@columbia.edu
Phone: 212-305-5778
Location: P&S-11-401



The research of the laboratory is aimed at the function of receptors and channels in terms of molecular structures. We try to understand how receptors recognize specific ligands, how the binding of these ligands is converted into the opening of ion-conducting channels, how the selectivity of the channels is determined, and how ions are conducted through the channels. The main approaches are to identify the residues that line the binding sites and conduction pathways and form the gates, to determine the three-dimensional structures, to locate the critical residues in these three-dimensional structures, and to detect structural changes in the transitions between functional states. To reach these goals, we use the methods of protein chemistry, molecular biology, and electrophysiology.

Selected Publications

Chung D, Chan P, Bankston J, Yang L, Liu G, Marx SO, Karlin A, Kass RS. Location of KCNE1 relative to KCNQ1 in the IKS potassium channel by disulfide crosslinking of substituted cysteines. Proc Natl Acad Sci USA, 2009 Jan 8. PMCID: PMC2630058

Wu R, Chudasama N, Zakharov SI, Doshi, D, Motoike H, Liu G, Deng S-X, Landry DW, Karlin A, Marx SO. Location of the beta4 transmembrane helices in the BK potassium channel. J. Neurosci 2009 Jul 1; 29:8321-8. PMCID: PMC2737688

Liu G, Niu X, Wu RS, Chudasama N, Yao Y, Jin X, Weinberg R, Zakharov SI, Motoike H, Marx SO, Karlin A. Location of modulatory beta subunits in BK potassium channels. J Gen Physiol. 2010 May;135(5):449-59. Epub 2010 Apr 12. PMCID: PMC2860586

Liu, G., Zakharov, S., Yang., L., Deng, S., Landry, D., Karlin, A., Marx, S. (2008) Position and role of the BK channel alpha subunit S0 helix inferred from disulfide crosslinking. J. Gen. Physiol 131: 537-548.

Liu, G., Zakharov, S., Yang., L., Wu, R., Deng, S., Landry, D., Karlin, A., Marx, S. (2008) Locations of the beta1 transmembrane helices in the BK potassium channel. Proc. Natl. Acad. Sci. USA 105:10727-10732.

Li, J., Shi, L., and Karlin, A. 2003. A photochemical approach to the lipid accessibility of engineered cysteinyl residues. Proc. Natl. Acad. Sci. USA 100: 886-891.

Yu, Y., Shi, L., and Karlin, A. 2003. Structural effects of quinacrine binding in the open channel of the acetylcholine receptor. Proc. Natl. Acad. Sci. USA 100: 3907-3912.

Karlin, A. 2002. Emerging structure of the nicotinic acetylcholine receptors. Nature Reviews Neuroscience 3: 102-114.