SmShb, the SH2-Containing Adaptor Protein ...
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
SmShb, the SH2-Containing Adaptor Protein B of Schistosoma mansoni Regulates Venus Kinase Receptor Signaling Pathways
Auteur(s) :
Morel, Marion [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vanderstraete, Mathieu [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Cailliau, Katia [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Hahnel, Steffen [Auteur]
Justus-Liebig-Universität Gießen = Justus Liebig University [JLU]
Grevelding, Christoph G. [Auteur]
Justus-Liebig-Universität Gießen = Justus Liebig University [JLU]
Dissous, Colette [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vanderstraete, Mathieu [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Cailliau, Katia [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Hahnel, Steffen [Auteur]
Justus-Liebig-Universität Gießen = Justus Liebig University [JLU]
Grevelding, Christoph G. [Auteur]
Justus-Liebig-Universität Gießen = Justus Liebig University [JLU]
Dissous, Colette [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Titre de la revue :
PLoS One
Numéro :
11
Pagination :
e0163283
Date de publication :
2016-09-16
ISSN :
1932-6203
Mot(s)-clé(s) en anglais :
Xenopus oocytes
phosphorylation
SH2 domains
immunoprecipitation
schistosoma mansoni
C-Jun N-terminal kinase signaling cascade
schistosoma
protein domains
phosphorylation
SH2 domains
immunoprecipitation
schistosoma mansoni
C-Jun N-terminal kinase signaling cascade
schistosoma
protein domains
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biologie cellulaire
Sciences du Vivant [q-bio]/Biologie cellulaire
Résumé en anglais : [en]
Venus kinase receptors (VKRs) are invertebrate receptor tyrosine kinases (RTKs) formed by an extracellular Venus Fly Trap (VFT) ligand binding domain associated via a transmembrane domain with an intracellular tyrosine ...
Lire la suite >Venus kinase receptors (VKRs) are invertebrate receptor tyrosine kinases (RTKs) formed by an extracellular Venus Fly Trap (VFT) ligand binding domain associated via a transmembrane domain with an intracellular tyrosine kinase (TK) domain. Schistosoma mansoni VKRs, SmVKR1 and SmVKR2, are both implicated in reproductive activities of the parasite. In this work, we show that the SH2 domain-containing protein SmShb is a partner of the phosphorylated form of SmVKR1. Expression of these proteins in Xenopus oocytes allowed us to demonstrate that the SH2 domain of SmShb interacts with the phosphotyrosine residue (pY979) located in the juxtamembrane region of SmVKR1. This interaction leads to phosphorylation of SmShb on tyrosines and promotes SmVKR1 signaling towards the JNK pathway. SmShb transcripts are expressed in all parasite stages and they were found in ovary and testes of adult worms, suggesting a possible colocalization of SmShb and SmVKR1 proteins. Silencing of SmShb in adult S. mansoni resulted in an accumulation of mature sperm in testes, indicating a possible role of SmShb in gametogenesis.Lire moins >
Lire la suite >Venus kinase receptors (VKRs) are invertebrate receptor tyrosine kinases (RTKs) formed by an extracellular Venus Fly Trap (VFT) ligand binding domain associated via a transmembrane domain with an intracellular tyrosine kinase (TK) domain. Schistosoma mansoni VKRs, SmVKR1 and SmVKR2, are both implicated in reproductive activities of the parasite. In this work, we show that the SH2 domain-containing protein SmShb is a partner of the phosphorylated form of SmVKR1. Expression of these proteins in Xenopus oocytes allowed us to demonstrate that the SH2 domain of SmShb interacts with the phosphotyrosine residue (pY979) located in the juxtamembrane region of SmVKR1. This interaction leads to phosphorylation of SmShb on tyrosines and promotes SmVKR1 signaling towards the JNK pathway. SmShb transcripts are expressed in all parasite stages and they were found in ovary and testes of adult worms, suggesting a possible colocalization of SmShb and SmVKR1 proteins. Silencing of SmShb in adult S. mansoni resulted in an accumulation of mature sperm in testes, indicating a possible role of SmShb in gametogenesis.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Équipe(s) de recherche :
Régulation des signaux de division
Date de dépôt :
2020-02-12T15:12:37Z
2021-03-19T14:06:36Z
2021-03-19T14:08:26Z
2021-03-19T14:06:36Z
2021-03-19T14:08:26Z
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