E
Eeva Sommer
Researcher at University of Dundee
Publications - 8
Citations - 891
Eeva Sommer is an academic researcher from University of Dundee. The author has contributed to research in topics: Phosphorylation & Protein kinase B. The author has an hindex of 7, co-authored 8 publications receiving 784 citations.
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Journal ArticleDOI
Characterization of VPS34-IN1, a selective inhibitor of Vps34, reveals that the phosphatidylinositol 3-phosphate-binding SGK3 protein kinase is a downstream target of class III phosphoinositide 3-kinase.
Ruzica Bago,Nazma Malik,Michael J. Munson,Alan R. Prescott,Paul Davies,Eeva Sommer,Natalia Shpiro,Richard J. Ward,Darren Cross,Ian G. Ganley,Dario R. Alessi +10 more
TL;DR: A highly selective and potent inhibitor of Vps34, termed VPS34-IN1, is described that inhibits Vps 34 with 25 nM IC50 in vitro, but does not significantly inhibit the activity of 340 protein kinases or 25 lipid kinases tested that include all isoforms of class I as well as class II PI3Ks.
Journal ArticleDOI
Protor-1 is required for efficient mTORC2-mediated activation of SGK1 in the kidney.
TL;DR: Results suggest that Protor-1 may play a role in enabling mTORC2 to efficiently activate SGK1, at least in the kidney.
Journal ArticleDOI
Elevated SGK1 predicts resistance of breast cancer cells to Akt inhibitors
Eeva Sommer,Hannah Dry,Darren Cross,Sylvie Guichard,Barry R. Davies,Barry R. Davies,Dario R. Alessi +6 more
TL;DR: The results of the present study suggest that monitoring SGK1 levels as well as responses of NDRG1 phosphorylation to Akt inhibitor administration could have a use in predicting the sensitivity of tumours to compounds that target Akt.
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Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1.
TL;DR: The small molecule GSK2334470 is described, which inhibits PDK1 with an IC₅₀ of ~10 nM, but does not suppress the activity of 93 other protein kinases including 13 AGC-kinases most related to PDK2 at 500-fold higher concentrations, and is suggested to be a useful tool for delineating the roles ofPDK1 in biological processes.
Journal ArticleDOI
PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12.
Xiaoqing Gan,Jiyong Wang,Chen Wang,Eeva Sommer,Tohru Kozasa,Tohru Kozasa,Srinivasa M. Srinivasula,Dario R. Alessi,Stefan Offermanns,Melvin I. Simon,Dianqing Wu +10 more
TL;DR: It is shown that lysophosphatidic acid (LPA) induces two phases of PKC-δ hydrophobic motif phosphorylation, which is critically important for fibroblast migration and pulmonary fibrosis development.