Phosphorylation target site specificity for AGC kinases DMPK E and Lats2.
until further notice
SourceJournal of Cellular Biochemistry, 113, 6, (2012), pp. 2126-2135
1 juni 2012
Article / Letter to editor
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Cell Biology (UMC)
Journal of Cellular Biochemistry
SubjectNCMLS 4: Energy and redox metabolism IGMD 8: Mitochondrial medicine; NCMLS 7: Chemical and physical biology; NCMLS 7: Chemical and physical biology DCN MP: Plasticity and memory
Serine/threonine kinases of the AGC group are important regulators of cell growth and motility. To examine the candidate substrate profile for two members of this group, DMPK E and Lats2, we performed in vitro kinase assays on peptide arrays. Substrate peptides for both kinases exhibited a predominance of basic residues surrounding the phosphorylation target site. 3D homology modeling of the kinase domains of DMPK E and Lats2 indicated that presence of two negative pockets in the peptide binding groove provides an explanation for the substrate preference. These findings will aid future research toward signaling functions of Lats2 and DMPK E within cells.
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