• Publications
  • Influence
Phosphorylation of the Protein Kinase Mutated in Peutz-Jeghers Cancer Syndrome, LKB1/STK11, at Ser431 by p90RSK and cAMP-dependent Protein Kinase, but Not Its Farnesylation at Cys433, Is Essential
TLDR
It is demonstrated that stimulation of Rat-2 or embryonic stem cells with activators of ERK1/2 or of cAMP-dependent protein kinase induced phosphorylation of endogenously expressed LKB1 at Ser431, and that full-length L KB1 expressed in 293 cells was prenylated by addition of a farnesyl group to Cys433. Expand
Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155.
TLDR
Ser(155) is identified as a third phosphorylation site on BAD and is the only residue in BAD that becomes phosphorylated when cells are exposed to cAMP-elevating agents, and prevents it from binding to Bcl-X(L) and promotes its interaction with 14-3-3 proteins. Expand
The insulin signalling pathway
TLDR
Although the understanding of the insulin signal transduction pathway is far from being complete, current knowledge of this pathway provides a framework for the development of novel drugs to treat diabetes and it is possible that drugs that mimic the effect that insulin has on its signalling pathway are orally effective. Expand
Identification of the sucrose non‐fermenting related kinase SNRK, as a novel LKB1 substrate
TLDR
This study identifies the sucrose non‐fermenting protein (SNF1)‐related kinase (SNRK), a largely unstudied AMPK subfamily member, as a novel substrate for LKB1, and demonstrates that Lkb1 activates SNRK by phosphorylating the T‐loop residue (Thr173), and that the LKB 1 regulatory subunits STRAD and MO25 are required for L KB1 to activate SNRk. Expand
Role of Semicarbazide-sensitive Amine Oxidase on Glucose Transport and GLUT4 Recruitment to the Cell Surface in Adipose Cells*
TLDR
It is proposed that SSAO activity might contribute through hydrogen peroxide production to the in vivo regulation of GLUT4 trafficking in adipose cells. Expand
High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
TLDR
The 2.0 Å crystal structure of the PDK1 kinase domain in complex with ATP defines the hydrophobic pocket termed the ‘PIF‐pocket’, which plays a key role in mediating the interaction and phosphorylation of certain substrates such as S6K1. Expand
Dopaminergic and Glutamatergic Signaling Crosstalk in Huntington's Disease Neurodegeneration: The Role of p25/Cyclin-Dependent Kinase 5
TLDR
It is demonstrated in knock-in HD striatal cells that mutant huntingtin enhances dopamine-mediated striatal cell death via dopamine D1 receptors, and p25/Cdk5 is identified as an important mediator of dopamine and glutamate neurotoxicity associated to HD. Expand
Molecular Basis for the Substrate Specificity of NIMA-related Kinase-6 (NEK6)
TLDR
This study provides the first description of the basis for the substrate specificity of NEK6 and indicates thatNEK6 is unlikely to be responsible for the IGF1-induced phosphorylation of the hydrophobic motif of S6K, SGK, and protein kinase B isoforms in vivo. Expand
Insulin-induced Drosophila S6 kinase activation requires phosphoinositide 3-kinase and protein kinase B.
TLDR
The results of the present study support the view that, in Drosophila cells, dPI3K and dPKB, as well dTOR, are required for the activation of dS6K by insulin. Expand
Interaction of PDK1 with Phosphoinositides Is Essential for Neuronal Differentiation but Dispensable for Neuronal Survival
TLDR
The integrity of the PDK1 PH domain was not essential to support the survival of different embryonic neuronal populations analyzed, and PKB-mediated phosphorylation of PRAS40 and TSC2, allowing optimal mTORC1 activation and brain-specific kinase (BRSK) protein synthesis, was markedly reduced in the mutant mice, leading to impaired neuronal growth and differentiation. Expand
...
1
2
3
4
5
...