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doi:10.22028/D291-27466
Titel: | The Phosphorylation of PDX-1 by Protein Kinase CK2 Is Crucial for Its Stability |
VerfasserIn: | Klein, Sabrina Meng, Rui Montenarh, Mathias Götz, Claudia |
Sprache: | Englisch |
Titel: | Pharmaceuticals |
Bandnummer: | 10 |
Heft: | 1 |
Verlag/Plattform: | MDPI |
Erscheinungsjahr: | 2016 |
DDC-Sachgruppe: | 610 Medizin, Gesundheit |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
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 der Erstveröffentlichung: | 10.3390/ph10010002 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-274660 hdl:20.500.11880/28560 http://dx.doi.org/10.22028/D291-27466 |
ISSN: | 1424-8247 |
Datum des Eintrags: | 10-Jan-2020 |
Fakultät: | M - Medizinische Fakultät |
Fachrichtung: | M - Medizinische Biochemie und Molekularbiologie |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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pharmaceuticals-10-00002.pdf | 2,78 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons