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Biophysical characterization of interactions between the C-termini of peripheral nerve claudins and the PDZ1 domain of zonula occludens.

Biochem Biophys Res Commun.. 2015-02; 
Wu J, Peng D, Zhang Y, Lu Z, Voehler M, Sanders CR, Li J. Department of Neurology, Vanderbilt University School of Medicine, USA.
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摘要

Our recent study has shown that cellular junctions in myelin and in the epi-/perineruium that encase nerve fibers regulate the permeability of the peripheral nerves. This permeability may affect propagation of the action potential. Direct interactions between the PDZ1 domain of zonula occludens (ZO1 or ZO2) and the C-termini of claudins are known to be crucial for the formation of tight junctions. Using the purified PDZ1 domain of ZO2 and a variety of C-terminal mutants of peripheral nerve claudins (claudin-1, claudin-2, claudin-3, claudin-5 in epi-/perineurium; claudin-19 in myelin), we have utilized NMR spectroscopy to determine specific roles of the 3 C-terminal claudin residues (position -2, -1, 0) for thei... More

关键词

Myelin junction; Myelin permeability; PMP22, peripheral myelin protein-22; PNS, peripheral nervous system; ZO1, zonula occludens-1; ZO2, zonula occludens-2
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