Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Gong, Yongfeng, Renigunta, Vijayaram, Zhou, Yi, Sunq, Abby, Wang, Jinzhi, Yang, Jing, Renigunta, Aparna, Baker, Lane A., Hou, Jianghui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
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
_version_ 1782403664476897280
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
work_keys_str_mv AT gongyongfeng biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT reniguntavijayaram biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT zhouyi biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT sunqabby biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT wangjinzhi biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT yangjing biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT reniguntaaparna biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT bakerlanea biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization
AT houjianghui biochemicalandbiophysicalanalysesoftightjunctionpermeabilitymadeofclaudin16andclaudin19dimerization