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Phosphorylation Dynamics during Early Differentiation of Human Embryonic Stem Cells

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Date
2009-08-07
ICR Author
Linding, Rune
Author
Van Hoof, D
Munoz, J
Braam, SR
Pinkse, MWH
Linding, R
Heck, AJR
Mummery, CL
Krijgsveld, J
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Type
Journal Article
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Abstract
Pluripotent stem cells, self-renew indefinitely and possess characteristic protein-protein networks that remodel during differentiation. How this occurs is poorly understood. Using quantitative mass spectrometry, we analyzed the (phospho)proteome of human embryonic stem cells (hESCs) during differentiation induced by bone morphogenetic protein (BMP) and removal of hESC growth factors. Of 5222 proteins identified, 1399 were phosphorylated on 3067 residues. Approximately 50% of these phosphosites were regulated within 1 hr of differentiation induction, revealing a complex interplay of phosphorylation networks spanning different signaling pathways and kinase activities. Among the phosphorylated proteins was the pluripotency-associated protein SOX2, which was SUMOylated as a result of phosphorylation. Using the data to predict kinase-substrate relationships, we reconstructed the hESC kinome, CDK1/2 emerged as central in controlling se renewal and lineage specification. The findings provide new insights into how hESCs exit the pluripotent state and present the hESC (phospho)proteome resource as a complement to existing pluripotency network databases.
URI
https://repository.icr.ac.uk/handle/internal/2404
DOI
https://doi.org/10.1016/j.stem.2009.05.021
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Language
eng
License start date
2009-08-07
Citation
CELL STEM CELL, 2009, 5 pp. 214 - 226
Publisher
CELL PRESS

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