3‐phosphoinositide‐dependent protein kinase ...
Document type :
Article dans une revue scientifique: Article original
DOI :
Permalink :
Title :
3‐phosphoinositide‐dependent protein kinase 1 (PDK1) mediates crosstalk between Src and Akt pathways in MET receptor signaling
Author(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
Journal title :
Febs Letters
Abbreviated title :
FEBS Lett
Publisher :
Wiley
Publication date :
2021-10-10
ISSN :
0014-5793
English keyword(s) :
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
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Collections :
Research team(s) :
Régulation des signaux de division
Submission date :
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
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