Phosphorylation target site specificity for AGC kinases DMPK E and Lats2 |
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Authors: | Gerrits Lieke Venselaar Hanka Wieringa Bé Wansink Derick G Hendriks Wiljan J A J |
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Affiliation: | Department of Cell Biology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. |
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Abstract: | 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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Keywords: | AGC KINASES DMPK KINASE SUBSTRATE Lats2 PEPTIDE ARRAY 3D HOMOLOGY MODELS |
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