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Phosphorylation target site specificity for AGC kinases DMPK E and lats2
Author(s) -
Gerrits Lieke,
Venselaar Hanka,
Wieringa Bé,
Wansink Derick G.,
Hendriks Wiljan J.A.J.
Publication year - 2012
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.24086
Subject(s) - kinase , phosphorylation , serine , threonine , peptide , biology , microbiology and biotechnology , protein serine threonine kinases , in vitro , biochemistry , protein kinase a
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. J. Cell. Biochem. 113: 2126–2135, 2012. © 2012 Wiley Periodicals, Inc.