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

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.

Pascual, J.M., and Karlin, A. 1998. State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor: Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the alpha subunit. J. Gen. Physiol. 111:717-739.

Zhang, H., and Karlin, A. 1998. Contribution of the beta subunit M2 segment to the ion-conducting pathway of the acetylcholine receptor. Biochemistry 37: 7952-7964. Wilson GG, and Karlin A (1998) The location of the gate in the acetylcholine receptor channel. Neuron 20:1269-1281.