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Updated: Jan 4, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

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Published on: February 21, 2019

Conserved Eukaryotic Kinase CK2 Chaperone Intrinsically Disordered Protein Interactions.

Lianhu Zhang¹, Dongmei Zhang¹, Dan Liu¹

¹State Key Laboratory for Ecological Pest Control of Fujian and Taiwan Crops, College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.

Applied and Environmental Microbiology

|November 3, 2019

Summary

Protein kinase CK2 (CK2) plays a key role in managing intrinsically disordered proteins (IDPs) by influencing their aggregation and binding to nucleic acids and other proteins.

Keywords:

Magnaporthe oryzae Pyricularia oryzae intrinsically disordered proteins protein interactions protein kinase CK2 transcriptomes

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Published on: September 2, 2019

Area of Science:

Biochemistry
Molecular Biology
Mycology

Background:

CK2 is a conserved eukaryotic serine/threonine kinase with numerous substrates.
CK2 has been shown to localize to nuclei and hyphal pores in Magnaporthe oryzae.
Intrinsically disordered proteins (IDPs) constitute a significant portion of eukaryotic proteomes and are crucial for various cellular functions.

Purpose of the Study:

To investigate the role of CK2 in protein aggregation and interactions.
To identify proteins interacting with the CK2 catalytic subunit MoCKa.
To explore the broader function of CK2 in protein-protein and protein-nucleic acid binding.

Main Methods:

Pulldown proteomics analysis of MoCKa in M. oryzae.
Bioinformatic analysis of transcriptomic data from M. oryzae and Fusarium graminearum.
Correlation analysis of CK2 expression with other cellular factors.

Main Results:

MoCKa pulldown enriched for septum, nucleolus, and IDP proteins with a CK2 phosphorylation motif.
CK2 phosphorylation motif is proposed to destabilize alpha-helices.
CKa expression positively correlated with Ser/Thr phosphatases, disaggregases (HSP104, YDJ1, SSA1), and ATG8.
High CKa expression suggests increased protein aggregate formation.

Conclusions:

CK2 phosphorylation and phosphatase dephosphorylation are involved in forming functional protein aggregates.
CK2 plays a general role in chaperoning the aggregation and disaggregation of IDPs.
CK2 mediates the binding of IDPs to proteins, DNA, and RNA, explaining its importance in cellular function and disease.