Please use this identifier to cite or link to this item: doi:10.22028/D291-27466
Title: The Phosphorylation of PDX-1 by Protein Kinase CK2 Is Crucial for Its Stability
Author(s): Klein, Sabrina
Meng, Rui
Montenarh, Mathias
Götz, Claudia
Language: English
Title: Pharmaceuticals
Volume: 10
Issue: 1
Publisher/Platform: MDPI
Year of Publication: 2016
DDC notations: 610 Medicine and health
Publikation type: Journal Article
Abstract: The homeodomain protein PDX-1 is a critical regulator of pancreatic development and insulin production in pancreatic β-cells. We have recently shown that PDX-1 is a substrate of protein kinase CK2; a multifunctional protein kinase which is implicated in the regulation of various cellular aspects, such as differentiation, proliferation, and survival. The CK2 phosphorylation site of PDX-1 is located within the binding region of the E3 ubiquitin ligase adaptor protein PCIF1. To study the interaction between PDX-1 and PCIF1 we used immunofluorescence analysis, co-immunoprecipitation, GST-pull-down studies, and proximity ligation assay (PLA). For the analysis of the stability of PDX-1 we performed a cycloheximide chase. We used PDX-1 in its wild-type form as well as phosphomutants of the CK2 phosphorylation site. In pancreatic β-cells PDX-1 binds to PCIF1. The phosphorylation of PDX-1 by CK2 increases the ratio of PCIF1 bound to PDX-1. The stability of PDX-1 is extended in the absence of CK2 phosphorylation. Our results identified protein kinase CK2 as new important modulator of the stability of PDX-1.
DOI of the first publication: 10.3390/ph10010002
Link to this record: urn:nbn:de:bsz:291--ds-274660
ISSN: 1424-8247
Date of registration: 10-Jan-2020
Faculty: M - Medizinische Fakultät
Department: M - Medizinische Biochemie und Molekularbiologie
Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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