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Molecular Basis for Cation Selectivity in Claudin‐2–Based Pores
Author(s) -
Yu Alan S. L.
Publication year - 2009
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2009.04023.x
Subject(s) - claudin , paracellular transport , selectivity , chemistry , tight junction , permeability (electromagnetism) , biophysics , microbiology and biotechnology , membrane , biochemistry , biology , catalysis
Claudins are transmembrane tight junction proteins that form paracellular pores. Claudins regulate the permeability of small inorganic ions and are selective on the basis of charge. We have developed an inducible expression system to measure the permeability of claudin‐2 and have found that claudin‐2 forms highly cation‐selective paracellular pores. The basis of this charge selectivity is likely to be the presence of a negatively charged binding site within the lumen of the pore. This may be a general mechanism by which claudins achieve selectivity.