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Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions
Integrin α6β4 is an essential, dynamic adhesion receptor for laminin 332 found on epithelial cells, required for formation of strong cell–extracellular matrix (ECM) adhesion and induced migration, and coordinated by regions of the β4C cytoplasmic domain. β4E, a unique splice variant of β4 expressed...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589785/ https://www.ncbi.nlm.nih.gov/pubmed/30865564 http://dx.doi.org/10.1091/mbc.E18-10-0652 |
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author | Wang, Mengdie Hinton, James P. Gard, Jaime M. C. Garcia, Joe G. N. Knudsen, Beatrice S. Nagle, Raymond B. Cress, Anne E. |
author_facet | Wang, Mengdie Hinton, James P. Gard, Jaime M. C. Garcia, Joe G. N. Knudsen, Beatrice S. Nagle, Raymond B. Cress, Anne E. |
author_sort | Wang, Mengdie |
collection | PubMed |
description | Integrin α6β4 is an essential, dynamic adhesion receptor for laminin 332 found on epithelial cells, required for formation of strong cell–extracellular matrix (ECM) adhesion and induced migration, and coordinated by regions of the β4C cytoplasmic domain. β4E, a unique splice variant of β4 expressed in normal tissue, contains a cytoplasmic domain of 231 amino acids with a unique sequence of 114 amino acids instead of β4C’s canonical 1089 amino acids. We determined the distribution of α6β4E within normal human glandular epithelium and its regulation and effect on cellular biophysical properties. Canonical α6β4C expressed in all basal cells, as expected, while α6β4E expressed within a subset of luminal cells. α6β4E expression was induced by three-dimensional culture conditions, activated Src, was reversible, and was stabilized by bortezomib, a proteasome inhibitor. α6β4C expressed in all cells during induced migration, whereas α6β4E was restricted to a subset of cells with increased kinetics of cell–cell and cell–ECM resistance properties. Interestingly, α6β4E presented in “ringlike” patterns measuring ∼1.75 × 0.72 microns and containing actin and CD9 at cell–ECM locations. In contrast, α6β4C expressed only within hemidesmosome-like structures containing BP180. Integrin α6β4E is an inducible adhesion isoform in normal epithelial cells that can alter biophysical properties of cell–cell and cell–ECM interactions. |
format | Online Article Text |
id | pubmed-6589785 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-65897852019-07-02 Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions Wang, Mengdie Hinton, James P. Gard, Jaime M. C. Garcia, Joe G. N. Knudsen, Beatrice S. Nagle, Raymond B. Cress, Anne E. Mol Biol Cell Articles Integrin α6β4 is an essential, dynamic adhesion receptor for laminin 332 found on epithelial cells, required for formation of strong cell–extracellular matrix (ECM) adhesion and induced migration, and coordinated by regions of the β4C cytoplasmic domain. β4E, a unique splice variant of β4 expressed in normal tissue, contains a cytoplasmic domain of 231 amino acids with a unique sequence of 114 amino acids instead of β4C’s canonical 1089 amino acids. We determined the distribution of α6β4E within normal human glandular epithelium and its regulation and effect on cellular biophysical properties. Canonical α6β4C expressed in all basal cells, as expected, while α6β4E expressed within a subset of luminal cells. α6β4E expression was induced by three-dimensional culture conditions, activated Src, was reversible, and was stabilized by bortezomib, a proteasome inhibitor. α6β4C expressed in all cells during induced migration, whereas α6β4E was restricted to a subset of cells with increased kinetics of cell–cell and cell–ECM resistance properties. Interestingly, α6β4E presented in “ringlike” patterns measuring ∼1.75 × 0.72 microns and containing actin and CD9 at cell–ECM locations. In contrast, α6β4C expressed only within hemidesmosome-like structures containing BP180. Integrin α6β4E is an inducible adhesion isoform in normal epithelial cells that can alter biophysical properties of cell–cell and cell–ECM interactions. The American Society for Cell Biology 2019-03-21 /pmc/articles/PMC6589785/ /pubmed/30865564 http://dx.doi.org/10.1091/mbc.E18-10-0652 Text en © 2019 Wang et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 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. |
spellingShingle | Articles Wang, Mengdie Hinton, James P. Gard, Jaime M. C. Garcia, Joe G. N. Knudsen, Beatrice S. Nagle, Raymond B. Cress, Anne E. Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title | Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title_full | Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title_fullStr | Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title_full_unstemmed | Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title_short | Integrin α6β4E variant is associated with actin and CD9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
title_sort | integrin α6β4e variant is associated with actin and cd9 structures and modifies the biophysical properties of cell–cell and cell–extracellular matrix interactions |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589785/ https://www.ncbi.nlm.nih.gov/pubmed/30865564 http://dx.doi.org/10.1091/mbc.E18-10-0652 |
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