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Updated: May 31, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
Published on: February 21, 2019
Adiponectin receptor 1 interacts with both subunits of protein kinase CK2
Cathleen Juhl1, Karin Mörl, Annette G Beck-Sickinger
1Institute of Biochemistry, Pharmacy and Psychology, Leipzig University, Leipzig, Germany.
Abstract:
Adiponectin is an adipose tissue-derived hormone that is involved in the inhibition of metabolic syndrome, protection of hypertension, and suppression of atherosclerosis. Since these effects are not understood in detail, adiponectin signaling has to be clarified for therapeutic applications. Adiponectin activities are mediated by its two receptors adiponectin receptor 1 and adiponectin receptor 2, which consist of seven transmembrane helices. Previous studies revealed the beta subunit of protein kinase CK2 as an interaction partner of the adiponectin receptor 1 N-terminus using a yeast-two-hybrid screen, co-immunoprecipitation, ELISA experiments, and co-localization studies. Inhibition of CK2 activity by 2-dimethylamino-4,5,6,7-tetrabromo-1H-benz-imidazole led to a decrease of ACC phosphorylation and indicates an important role of CK2 in adiponectin signaling. CK2 is characterized as a heterotetramer that consists of two regulatory beta and two catalytic alpha subunits, but a holoenzyme-independent role for both subunits is described as well. Therefore, we analyzed the role of the catalytic subunit in this interaction by co-immunoprecipitation and bimolecular fluorescence complementation studies and found CK2 alpha as an interaction partner of the receptor. Treatment with full-length adiponectin resulted in no dissociation of the catalytic alpha subunit. Consequently, our data suggest an interaction of the adiponectin receptor 1 with the tetrameric complex and identified protein kinase CK2 as a key player in adiponectin signaling.
Insights
Protein kinase CK2 interacts with adiponectin receptor 1, revealing a key role for CK2 in adiponectin signaling pathways. This discovery aids understanding of adiponectin
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Adiponectin, an adipose hormone, regulates metabolic syndrome, hypertension, and atherosclerosis.
- Adiponectin's therapeutic potential necessitates a detailed understanding of its signaling pathways.
- Adiponectin receptors (AdipoR1/2) mediate adiponectin's biological activities.
Purpose of the Study:
- To elucidate the detailed molecular mechanisms of adiponectin signaling.
- To identify specific interaction partners of adiponectin receptor 1 (AdipoR1).
- To clarify the role of protein kinase CK2 in adiponectin signaling.
Main Methods:
- Yeast-two-hybrid screening
- Co-immunoprecipitation assays
- ELISA experiments
- Co-localization studies
- Bimolecular fluorescence complementation (BiFC)
- Pharmacological inhibition of CK2 activity
Main Results:
- The beta subunit of protein kinase CK2 was identified as an AdipoR1 interaction partner.
- CK2 inhibition decreased ACC phosphorylation, implicating CK2 in adiponectin signaling.
- The catalytic alpha subunit of CK2 also interacts with AdipoR1.
- Full-length adiponectin did not induce dissociation of the CK2 alpha subunit from AdipoR1.
Conclusions:
- Adiponectin receptor 1 interacts with the tetrameric complex of protein kinase CK2.
- Protein kinase CK2 is a crucial component in adiponectin signaling pathways.
- These findings provide a basis for therapeutic applications targeting adiponectin signaling.
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