3‐phosphoinositide‐dependent protein kinase ...
Type de document :
Article dans une revue scientifique: Article original
DOI :
URL permanente :
Titre :
3‐phosphoinositide‐dependent protein kinase 1 (PDK1) mediates crosstalk between Src and Akt pathways in MET receptor signaling
Auteur(s) :
Molinaro, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Martoriati, Alain [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Lescuyer, Arlette [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Fliniaux, Ingrid [Auteur]
Physiologie Cellulaire (PHYCEL) - U1003
Physiologie Cellulaire (PHYCEL) - U1003
Tulasne, David [Auteur]
Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290
Cancer Heterogeneity, Plasticity and Resistance to Therapies (CANTHER) - UMR 9020 - UMR 1277
Cailliau, Katia [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Martoriati, Alain [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Lescuyer, Arlette [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Fliniaux, Ingrid [Auteur]

Physiologie Cellulaire (PHYCEL) - U1003
Physiologie Cellulaire (PHYCEL) - U1003
Tulasne, David [Auteur]

Miniaturisation pour la Synthèse, l'Analyse et la Protéomique (MSAP) - USR 3290
Cancer Heterogeneity, Plasticity and Resistance to Therapies (CANTHER) - UMR 9020 - UMR 1277
Cailliau, Katia [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Titre de la revue :
Febs Letters
Nom court de la revue :
FEBS Lett
Éditeur :
Wiley
Date de publication :
2021-10-10
ISSN :
0014-5793
Mot(s)-clé(s) en anglais :
Akt
G2/M transition
hepatocyte growth factor receptor
MET signaling
PDK1
Src
Xenopus oocyte
G2/M transition
hepatocyte growth factor receptor
MET signaling
PDK1
Src
Xenopus oocyte
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
The high-affinity tyrosine kinase receptor MET plays a pivotal role in several facets of cell regulation. Although its mitogenic effect is well documented, some aspects of connection patterns between signaling pathways ...
Lire la suite >The high-affinity tyrosine kinase receptor MET plays a pivotal role in several facets of cell regulation. Although its mitogenic effect is well documented, some aspects of connection patterns between signaling pathways involved in cell cycle progression remain to be deciphered. We have used a tractable heterologous expression system, the Xenopus oocyte, to detect connections between distinct MET signaling cascades involved in G2/M progression. Our results reveal that Src acts as an adapter via its SH2 domain to recruit 3-phosphoinositide-dependent protein kinase 1 (PDK1) to the MET signaling complex leading to Akt phosphorylation. These data define an original crosstalk between Src and Akt signaling pathways that contributes to MET-induced entry into the M phase, and deserves further investigation in pathologies harboring deregulation of this receptor.Lire moins >
Lire la suite >The high-affinity tyrosine kinase receptor MET plays a pivotal role in several facets of cell regulation. Although its mitogenic effect is well documented, some aspects of connection patterns between signaling pathways involved in cell cycle progression remain to be deciphered. We have used a tractable heterologous expression system, the Xenopus oocyte, to detect connections between distinct MET signaling cascades involved in G2/M progression. Our results reveal that Src acts as an adapter via its SH2 domain to recruit 3-phosphoinositide-dependent protein kinase 1 (PDK1) to the MET signaling complex leading to Akt phosphorylation. These data define an original crosstalk between Src and Akt signaling pathways that contributes to MET-induced entry into the M phase, and deserves further investigation in pathologies harboring deregulation of this receptor.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
CNRS
Collections :
Équipe(s) de recherche :
Régulation des signaux de division
Date de dépôt :
2021-10-15T13:43:24Z
2021-10-18T08:37:43Z
2022-01-31T10:11:13Z
2021-10-18T08:37:43Z
2022-01-31T10:11:13Z
Fichiers
- P21.32 17214995.pdf
- Version soumise (preprint)
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