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Published online before print October 26, 2007, 10.1110/ps.072874607
Protein Science (2007), 16:2711-2715. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Protein kinase C delta is phosphorylated on five novel Ser/Thr sites following inducible overexpression in human colorectal cancer cells

Arkadiusz Welman1,3, John R. Griffiths2,3, Anthony D. Whetton2, and Caroline Dive1

1 Cancer Research UK, Clinical and Experimental Pharmacology Group, Paterson Institute for Cancer Research, University of Manchester, Manchester M20 4BX, United Kingdom
2 Stem Cell and Leukaemia Proteomics Laboratory, Division of Cancer Studies, University of Manchester, Kinnaird House, Manchester, M20 4QL, United Kingdom

(RECEIVED March 12, 2007; FINAL REVISION July 31, 2007; ACCEPTED September 4, 2007)

Phosphorylation plays an important role in regulation of protein kinase C delta (PKC{delta}). To date, three Ser/Thr residues (Thr 505, Ser 643, and Ser 662) and nine tyrosine residues (Tyr 52, Tyr 64, Tyr 155, Tyr 187, Tyr 311, Tyr 332, Tyr 512, Tyr 523, and Tyr 565) have been defined as regulatory phosphorylation sites for this protein (rat PKC{delta} numbering). We combined doxycycline-regulated inducible gene expression technology with a hypothesis-driven mass spectrometry approach to study PKC{delta} phosphorylation pattern in colorectal cancer cells. We report identification of five novel Ser/Thr phosphorylation sites: Thr 50, Thr 141, Ser 304, Thr 451, and Ser 506 (human PKC{delta} numbering) following overexpression of PKC{delta} in HCT116 human colon carcinoma cells grown in standard tissue culture conditions. Identification of potential novel phosphorylation sites will affect further functional studies of this protein, and may introduce additional complexity to PKC{delta} signaling.

Keywords: PKC{delta}; phosphorylation; colon cancer; HCT116; Tet on; MIDAS; mass spectrometry


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