Description
The protein level of OCT4, a core pluripotency transcriptional factor, is vital for embryonic stem cell (ESC) maintenance, differentiation and somatic cell reprogramming. Although OCT4 protein is regulated at multiple scales, the role and regulatory mechanisms of OCT4 ubiquitination in reprogramming remains elusive. We identified the five lysine residues as ubiquitination sites on OCT4, and found that destruction of the ubiquitination can enhance OCT4 activity in reprogramming.