Phosphoproteomics Profiling Suggests a Role for Nuclear βΙPKC in Transcription Processes of Undifferentiated Murine Embryonic Stem Cells
journal contributionposted on 03.12.2010, 00:00 by Helio Miranda Costa-Junior, Nicole Milaré Garavello, Mariana Lemos Duarte, Denise Aparecida Berti, Talita Glaser, Alexander de Andrade, Carlos A. Labate, André Teixeira da Silva Ferreira, Jonas Enrique Aguilar Perales, José Xavier-Neto, José Eduardo Krieger, Deborah Schechtman
Any type of content formally published in an academic journal, usually following a peer-review process.
Protein kinase C (PKC) plays a key role in embryonic stem cell (ESC) proliferation, self-renewal, and differentiation. However, the function of specific PKC isoenzymes have yet to be determined. Of the PKCs expressed in undifferentiated ESCs, βIPKC was the only isoenzyme abundantly expressed in the nuclei. To investigate the role of βΙPKC in these cells, we employed a phosphoproteomics strategy and used two classical (cPKC) peptide modulators and one βIPKC-specific inhibitor peptide. We identified 13 nuclear proteins that are direct or indirect βΙPKC substrates in undifferentiated ESCs. These proteins are known to be involved in regulating transcription, splicing, and chromatin remodeling during proliferation and differentiation. Inhibiting βΙPKC had no effect on DNA synthesis in undifferentiated ESCs. However, upon differentiation, many cells seized to express βΙPKC and βΙPKC was frequently found in the cytoplasm. Taken together, our results suggest that βIPKC takes part in the processes that maintain ESCs in their undifferentiated state.