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Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization
The molecular nature of tight junction architecture and permeability is a long-standing mystery. Here, by comprehensive biochemical, biophysical, genetic, and electron microscopic analyses of claudin-16 and -19 interactions—two claudins that play key polygenic roles in fatal human renal disease, FHH...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666130/ https://www.ncbi.nlm.nih.gov/pubmed/26446843 http://dx.doi.org/10.1091/mbc.E15-06-0422 |
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author | Gong, Yongfeng Renigunta, Vijayaram Zhou, Yi Sunq, Abby Wang, Jinzhi Yang, Jing Renigunta, Aparna Baker, Lane A. Hou, Jianghui |
author_facet | Gong, Yongfeng Renigunta, Vijayaram Zhou, Yi Sunq, Abby Wang, Jinzhi Yang, Jing Renigunta, Aparna Baker, Lane A. Hou, Jianghui |
author_sort | Gong, Yongfeng |
collection | PubMed |
description | The molecular nature of tight junction architecture and permeability is a long-standing mystery. Here, by comprehensive biochemical, biophysical, genetic, and electron microscopic analyses of claudin-16 and -19 interactions—two claudins that play key polygenic roles in fatal human renal disease, FHHNC—we found that 1) claudin-16 and -19 form a stable dimer through cis association of transmembrane domains 3 and 4; 2) mutations disrupting the claudin-16 and -19 cis interaction increase tight junction ultrastructural complexity but reduce tight junction permeability; and 3) no claudin hemichannel or heterotypic channel made of claudin-16 and -19 trans interaction can exist. These principles can be used to artificially alter tight junction permeabilities in various epithelia by manipulating selective claudin interactions. Our study also emphasizes the use of a novel recording approach based on scanning ion conductance microscopy to resolve tight junction permeabilities with submicrometer precision. |
format | Online Article Text |
id | pubmed-4666130 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-46661302016-02-16 Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization Gong, Yongfeng Renigunta, Vijayaram Zhou, Yi Sunq, Abby Wang, Jinzhi Yang, Jing Renigunta, Aparna Baker, Lane A. Hou, Jianghui Mol Biol Cell Articles The molecular nature of tight junction architecture and permeability is a long-standing mystery. Here, by comprehensive biochemical, biophysical, genetic, and electron microscopic analyses of claudin-16 and -19 interactions—two claudins that play key polygenic roles in fatal human renal disease, FHHNC—we found that 1) claudin-16 and -19 form a stable dimer through cis association of transmembrane domains 3 and 4; 2) mutations disrupting the claudin-16 and -19 cis interaction increase tight junction ultrastructural complexity but reduce tight junction permeability; and 3) no claudin hemichannel or heterotypic channel made of claudin-16 and -19 trans interaction can exist. These principles can be used to artificially alter tight junction permeabilities in various epithelia by manipulating selective claudin interactions. Our study also emphasizes the use of a novel recording approach based on scanning ion conductance microscopy to resolve tight junction permeabilities with submicrometer precision. The American Society for Cell Biology 2015-12-01 /pmc/articles/PMC4666130/ /pubmed/26446843 http://dx.doi.org/10.1091/mbc.E15-06-0422 Text en © 2015 Gong, Renigunta, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Gong, Yongfeng Renigunta, Vijayaram Zhou, Yi Sunq, Abby Wang, Jinzhi Yang, Jing Renigunta, Aparna Baker, Lane A. Hou, Jianghui Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title | Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title_full | Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title_fullStr | Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title_full_unstemmed | Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title_short | Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
title_sort | biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666130/ https://www.ncbi.nlm.nih.gov/pubmed/26446843 http://dx.doi.org/10.1091/mbc.E15-06-0422 |
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