N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.

α6ß4 integrin is an essential component of hemidesmosomes and modulates cell migration in wound healing and cancer invasion. To elucidate the role of N-glycosylation on ß4 integrin, we investigated keratinocyte adhesion and migration through the re-expression of wild-type or N-glycosylation-defectiv...

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Autores principales:	Yoshinobu Kariya, Jianguo Gu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8d2f06ef10954a269cd28d18394d284c
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spelling	oai:doaj.org-article:8d2f06ef10954a269cd28d18394d284c2021-11-18T07:35:08ZN-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.1932-620310.1371/journal.pone.0027084https://doaj.org/article/8d2f06ef10954a269cd28d18394d284c2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22073258/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203α6ß4 integrin is an essential component of hemidesmosomes and modulates cell migration in wound healing and cancer invasion. To elucidate the role of N-glycosylation on ß4 integrin, we investigated keratinocyte adhesion and migration through the re-expression of wild-type or N-glycosylation-defective ß4 integrin (ΔNß4) in ß4 integrin null keratinocytes. N-glycosylation of ß4 integrin was not essential for the heterodimer formation of ß4 integrin with α6 integrin and its expression on a cell surface, but N-glycosylation was required for integrin-mediated cell adhesion and migration. Concomitantly with the reduction of ß4 integrin in the membrane microdomain, the intracellular signals of Akt and ERK activation were decreased in cells expressing ΔNß4 integrin. Forced cross-linking of ß4 integrin rescued the decreased ERK activation in ΔNß4 integrin-expressing cells to a similar extent in wild-type ß4 integrin-expressing cells. Surprisingly, compared with cells expressing wild-type ß4 integrin, an alternation in N-glycan structures expressed on epidermal growth factor receptor (EGFR), and the induction of a stronger association between EGFR and ß4 integrin were observed in ΔNß4 integrin-expressing cells. These results clearly demonstrated that N-glycosylation on ß4 integrin plays an essential role in keratinocyte cellular function by allowing the appropriate complex formation on cell surfaces.Yoshinobu KariyaJianguo GuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27084 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yoshinobu Kariya Jianguo Gu N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
description	α6ß4 integrin is an essential component of hemidesmosomes and modulates cell migration in wound healing and cancer invasion. To elucidate the role of N-glycosylation on ß4 integrin, we investigated keratinocyte adhesion and migration through the re-expression of wild-type or N-glycosylation-defective ß4 integrin (ΔNß4) in ß4 integrin null keratinocytes. N-glycosylation of ß4 integrin was not essential for the heterodimer formation of ß4 integrin with α6 integrin and its expression on a cell surface, but N-glycosylation was required for integrin-mediated cell adhesion and migration. Concomitantly with the reduction of ß4 integrin in the membrane microdomain, the intracellular signals of Akt and ERK activation were decreased in cells expressing ΔNß4 integrin. Forced cross-linking of ß4 integrin rescued the decreased ERK activation in ΔNß4 integrin-expressing cells to a similar extent in wild-type ß4 integrin-expressing cells. Surprisingly, compared with cells expressing wild-type ß4 integrin, an alternation in N-glycan structures expressed on epidermal growth factor receptor (EGFR), and the induction of a stronger association between EGFR and ß4 integrin were observed in ΔNß4 integrin-expressing cells. These results clearly demonstrated that N-glycosylation on ß4 integrin plays an essential role in keratinocyte cellular function by allowing the appropriate complex formation on cell surfaces.
format	article
author	Yoshinobu Kariya Jianguo Gu
author_facet	Yoshinobu Kariya Jianguo Gu
author_sort	Yoshinobu Kariya
title	N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
title_short	N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
title_full	N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
title_fullStr	N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
title_full_unstemmed	N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
title_sort	n-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/8d2f06ef10954a269cd28d18394d284c
work_keys_str_mv	AT yoshinobukariya nglycosylationofß4integrincontrolstheadhesionandmotilityofkeratinocytes AT jianguogu nglycosylationofß4integrincontrolstheadhesionandmotilityofkeratinocytes
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N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.

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