PMID: 21406692 RLIMS-P 1 Check other iTextMine results Issue Report
Title
| 1. | System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. |
Abstract
| 2. | To elucidate cellular events underlying the pluripotency of human embryonic stem cells (hESCs), we performed parallel quantitative proteomic and phosphoproteomic analyses of hESCs during differentiation initiated by a diacylglycerol analog or transfer to media that had not been conditioned by feeder cells. |
| 3. | We profiled 6521 proteins and 23,522 phosphorylation sites, of which almost 50% displayed dynamic changes in phosphorylation status during 24 hours of differentiation. |
| 4. | These data are a resource for studies of the events associated with the maintenance of hESC pluripotency and those accompanying their differentiation. |
| 5. | From these data, we identified a core hESC phosphoproteome of sites with similar robust changes in response to the two distinct treatments. |
| 6. | These sites exhibited distinct dynamic phosphorylation patterns, which were linked to known or predicted kinases on the basis of the matching sequence motif. |
| 7. | In addition to identifying previously unknown phosphorylation sites on factors associated with differentiation, such as kinases and transcription factors, we observed dynamic phosphorylation of DNA methyltransferases (DNMTs). |
| 8. | We found a specific interaction of DNMTs during early differentiation with the PAF1 (polymerase-associated factor 1) transcriptional elongation complex, which binds to promoters of the pluripotency and known DNMT target genes encoding OCT4 and NANOG, thereby providing a possible molecular link for the silencing of these genes during differentiation. |
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Legend: SUBSTRATE KINASE INTERACTANT SITE GENE MIRNA ANOMALY EXPRESSION DISEASE OUTCOME/RESPONSE SR_DRUG DRUG CELL TRIGGER Normalized
Tool: RLIMS-P
| PTM enzyme | Substrate | Site | Sentence |
|---|---|---|---|
| DNA methyltransferases (DNMTs) | 7 |