Related Experiment Video

Updated: Aug 8, 2026

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors
12:40

A Method for Screening and Validation of Resistant Mutations Against Kinase Inhibitors

Published on: December 7, 2014

Validation of protein kinase CK2 as oncological target

S Seeber1, O G Issinger, T Holm

  • 1Roche Diagnostics GmbH, Pharma Research Penzberg, Nonnenwald 2, D-82377 Penzberg, Germany.

Apoptosis : an International Journal on Programmed Cell Death
|September 1, 2005
PubMed

Insights

Protein kinase CK2 (casein kinase 2) is elevated in tumors. Depleting CK2 catalytic subunits did not induce apoptosis, suggesting CK2 is not sufficient to trigger programmed cell death.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein kinase CK2 (casein kinase 2) is a highly conserved enzyme implicated in cellular transformation.
  • Its role in apoptosis and cell survival remains controversial, with conflicting experimental results.
  • CK2 activity is elevated in various tumor types and highly proliferating tissues.

Purpose of the Study:

  • To investigate the role of CK2 in programmed cell death.
  • To elucidate whether CK2 catalytic subunits are essential for triggering apoptosis.

Main Methods:

  • Depletion of CK2 catalytic subunits using antisense oligodeoxynucleotides and siRNA techniques.
  • Assessment of CK2 kinase activity and its impact on apoptosis.

Main Results:

  • Protein kinase CK2 exhibits remarkable stability, potentially due to protein associations, extended half-life, or reduced proteolytic degradation.
  • Effective reduction of CK2 kinase activity was achieved in all investigated cells.
  • CK2 depletion alone was insufficient to induce enhanced drug-induced apoptosis.

Conclusions:

  • Protein kinase CK2 possesses high intrinsic stability.
  • CK2 may not be the sole factor required to trigger drug-induced apoptosis.
  • Further research is needed to fully understand CK2's role in cell death pathways.

More Related Videos

Assaying Protein Kinase Activity with Radiolabeled ATP08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...