Non-C-mannosylable mucin CYS domains ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
Non-C-mannosylable mucin CYS domains hindered proper folding and secretion of mucin.
Auteur(s) :
Gouyer, Valérie [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Demouveaux, Bastien [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Lacroix, Guillaume [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Valque, Helene [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
gottrand, Fréderic [Auteur]
Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Desseyn, Jean-Luc [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Lille Inflammation Research International Center - U 995 [LIRIC]
Demouveaux, Bastien [Auteur]

Lille Inflammation Research International Center - U 995 [LIRIC]
Lacroix, Guillaume [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Valque, Helene [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
gottrand, Fréderic [Auteur]

Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Desseyn, Jean-Luc [Auteur]

Lille Inflammation Research International Center - U 995 [LIRIC]
Titre de la revue :
Biochemical and biophysical research communications
Nom court de la revue :
Biochem. Biophys. Res. Commun.
Numéro :
506
Pagination :
812-818
Date de publication :
2018-10-30
ISSN :
1090-2104
Mot(s)-clé(s) :
Mucin
C-mannosylation
CYS domain
C-mannosylation
CYS domain
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
The CYS domain occurs in multiple copies in many gel-forming mucins. It is believed that CYS domains can interact with each other in a reversible manner, suggesting a key role of the domain in gel formation. This domain ...
Lire la suite >The CYS domain occurs in multiple copies in many gel-forming mucins. It is believed that CYS domains can interact with each other in a reversible manner, suggesting a key role of the domain in gel formation. This domain always contains in its amino-terminal sequence the C-mannosylation motif WXXW, but whether the CYS domain is C-mannosylated is debated, and the putative role of C-mannosylation of the domain is unclear. We prepared recombinant CYS domains of the human mucin MUC5B with (WXXW→AXXW) and without a single amino acid mutation and mini-5B mucins made of a large Ser/Thr/Pro region flanked by two CYS domains with the WXXW motif or with the mutated AXXW motif on the first, second or both CYS domains. We found that the single CYS domain and the two CYS domains of mini-5B mucin must be C-mannosylable for the efficient maturation and secretion of the recombinant molecules; otherwise, they are retained in the cell and co-localized with a resident enzyme of the endoplasmic reticulum.Lire moins >
Lire la suite >The CYS domain occurs in multiple copies in many gel-forming mucins. It is believed that CYS domains can interact with each other in a reversible manner, suggesting a key role of the domain in gel formation. This domain always contains in its amino-terminal sequence the C-mannosylation motif WXXW, but whether the CYS domain is C-mannosylated is debated, and the putative role of C-mannosylation of the domain is unclear. We prepared recombinant CYS domains of the human mucin MUC5B with (WXXW→AXXW) and without a single amino acid mutation and mini-5B mucins made of a large Ser/Thr/Pro region flanked by two CYS domains with the WXXW motif or with the mutated AXXW motif on the first, second or both CYS domains. We found that the single CYS domain and the two CYS domains of mini-5B mucin must be C-mannosylable for the efficient maturation and secretion of the recombinant molecules; otherwise, they are retained in the cell and co-localized with a resident enzyme of the endoplasmic reticulum.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Inserm
Université de Lille
CHU Lille
Université de Lille
CHU Lille
Équipe(s) de recherche :
Nutritional modulation of inflammation and infection
Date de dépôt :
2019-03-01T14:35:21Z
2019-06-06T11:46:52Z
2021-05-14T10:47:42Z
2022-02-09T07:27:11Z
2022-11-08T10:32:50Z
2019-06-06T11:46:52Z
2021-05-14T10:47:42Z
2022-02-09T07:27:11Z
2022-11-08T10:32:50Z
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