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Anudharan Balendran
Researcher at University of Dundee
Publications - 8
Citations - 1815
Anudharan Balendran is an academic researcher from University of Dundee. The author has contributed to research in topics: ASK1 & MAP2K7. The author has an hindex of 7, co-authored 8 publications receiving 1772 citations.
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Journal ArticleDOI
The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells.
Michayla R. Williams,J. Simon C. Arthur,Anudharan Balendran,Jeroen van der Kaay,Valeria Poli,Philip Cohen,Dario R. Alessi +6 more
TL;DR: PDK1 mediates activation of PKB, p70 S6 kinase and p90 Rsk in vivo, but is not rate-limiting foractivation of PKA, MSK1 and AMPK.
Journal ArticleDOI
PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
Anudharan Balendran,Antonio Casamayor,Maria Deak,Andrew D. Paterson,Piers R. J. Gaffney,Richard A. Currie,C. Peter Downes,Dario R. Alessi +7 more
TL;DR: PDK1 and PDK2 might be the same enzyme, the substrate specificity and activity of PDK1 being regulated through its interaction with another protein(s), and PRK2 is a probable substrate for PDK 1.
Journal ArticleDOI
Ceramide impairs the insulin-dependent membrane recruitment of protein kinase B leading to a loss in downstream signalling in L6 skeletal muscle cells.
Eric Hajduch,Anudharan Balendran,Ian H. Batty,Gary J. Litherland,Anne S. Blair,C P Downes,Harinder S. Hundal +6 more
TL;DR: It is suggested that a defect in protein kinase B recruitment underpins the ceramide-induced loss in insulin sensitivity of key cell responses such as glucose transport and glycogen synthesis in L6 cells and that a stimulated rise in PtdIns(3,4,5)P3 is necessary but not sufficient for protein Kinase B activation in this system.
Journal ArticleDOI
Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms
TL;DR: It is demonstrated that in embryonic stem (ES) cells lacking PDK1 (PDK1−/− cells), the intracellular levels of endogenously expressed PKCα,PKCβI, PKCγ, PK Cδ, PK cδ and PKCϵ, and PKc‐related kinase‐1 (PRK1) are vastly reduced compared to control ES cells (PDk1+/+ cells).
Journal ArticleDOI
A 3-Phosphoinositide-dependent Protein Kinase-1 (PDK1) Docking Site Is Required for the Phosphorylation of Protein Kinase Cζ (PKCζ) and PKC-related Kinase 2 by PDK1
Anudharan Balendran,Ricardo M. Biondi,Peter C. F. Cheung,Antonio Casamayor,Maria Deak,Dario R. Alessi +5 more
TL;DR: Findings indicate that the hydrophobic motif of PRK2 and PKCζ acts as a “docking site” enabling the recruitment of PDK1 to these substrates, essential for their phosphorylation byPDK1 in cells.