AI Article Synopsis
- NANOG is a key protein that helps maintain the ability of stem cells to stay undifferentiated and self-renewing, but its regulation after being made (posttranslational regulation) isn't well understood.* -
- Researchers found eleven phosphorylation sites on human NANOG, with nine of them affecting single amino acids, which can influence its function.* -
- To uncover the kinases responsible for these modifications, they created a new assay called MAKS that can test multiple kinases at once, revealing that ERK2 and CDK1/CyclinA2 specifically phosphorylate NANOG.*
Article Abstract
NANOG is a divergent homeobox protein and a core component of the transcriptional circuitry that sustains pluripotency and self-renewal. Although NANOG has been extensively studied on the transcriptional level, little is known regarding its posttranslational regulation, likely due to its low abundance and challenging physical properties. Here, we identify eleven phosphorylation sites on endogenous human NANOG, nine of which mapped to single amino acids. To screen for the signaling molecules that impart these modifications, we developed the multiplexed assay for kinase specificity (MAKS). MAKS simultaneously tests activity for up to ten kinases while directly identifying the substrate and exact site of phosphorylation. Using MAKS, we discovered site-specific phosphorylation by ERK2 and CDK1/CyclinA2, providing a putative link between key signaling pathways and NANOG.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3966117 | PMC |
| http://dx.doi.org/10.1016/j.stemcr.2013.12.005 | DOI Listing |
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