Background: Self-renewal properties are attributed to critical amounts of the OCT4A transcription factor, and little is known about its post-translational regulation. Results: OCT4A interacts with ERK1/2 and is phosphorylated at Ser-111, increasing its ubiquitination and degradation. Discussion: These results suggest an increase in OCT4A degradation downstream of MEK1 activation and FGF2 treatment. Significance: Controlling the mechanism by which cells balance self-renewal would advance our knowledge of stem cells. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Serine 111 phosphorylation regulates OCT4A protein subcellular distribution and degradation
Ferro F.Conceptualization
;
2012-01-01
Abstract
Background: Self-renewal properties are attributed to critical amounts of the OCT4A transcription factor, and little is known about its post-translational regulation. Results: OCT4A interacts with ERK1/2 and is phosphorylated at Ser-111, increasing its ubiquitination and degradation. Discussion: These results suggest an increase in OCT4A degradation downstream of MEK1 activation and FGF2 treatment. Significance: Controlling the mechanism by which cells balance self-renewal would advance our knowledge of stem cells. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.File in questo prodotto:
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