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. 2016 Dec 28;10(1):2. doi: 10.3390/ph10010002

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© 2016 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Model of the PDX-1-PCIF1 interaction (a) CK2 phosphorylates mouse PDX-1 at threonine 231 and serine 232. This site is located in the middle of a phosphodegron, which binds the E3 ubiquitin ligase protein PCIF1 in a phosphorylated form. PCIF1 targets PDX-1 to the proteasome where it is ubiquitinated and subsequently degraded; and (b) upon CK2 inhibition, T231 and S232 of PDX-1 are not phosphorylated. As these important residues of the phosphodegron are not phosphorylated, the interaction with PCIF1 is reduced and PDX-1 is more stable.