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Published online May 12, 2008
doi:10.1083/jcb.200711165
The Journal of Cell Biology, Vol. 181, No. 4, 683-695
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Shen et al.
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Article

 The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state

Le Shen, Christopher R. Weber, and Jerrold R. Turner

Department of Pathology, The University of Chicago, Chicago, IL 60637

Correspondence to Jerrold R. Turner: jturner{at}bsd.uchicago.edu

The tight junction defines epithelial organization. Structurally, the tight junction is comprised of transmembrane and membrane-associated proteins that are thought to assemble into stable complexes to determine function. In this study, we measure tight junction protein dynamics in live confluent Madin–Darby canine kidney monolayers using fluorescence recovery after photobleaching and related methods. Mathematical modeling shows that the majority of claudin-1 (76 ± 5%) is stably localized at the tight junction. In contrast, the majority of occludin (71 ± 3%) diffuses rapidly within the tight junction with a diffusion constant of 0.011 µm2s–1. Zonula occludens-1 molecules are also highly dynamic in this region, but, rather than diffusing within the plane of the membrane, 69 ± 5% exchange between membrane and intracellular pools in an energy-dependent manner. These data demonstrate that the tight junction undergoes constant remodeling and suggest that this dynamic behavior may contribute to tight junction assembly and regulation.

Abbreviations used in this paper: FLIP, fluorescent loss in photobleaching; MBCD, methyl-β-cyclodextrin; PA, photoactivable; TER. transepithelial resistance; ZO, zonula occludens.

© 2008 Shen et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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