Related Experiment Video

Updated: Aug 20, 2026

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

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

The antiapoptotic protein ICBP90 is a target for protein kinase 2

Christian Bronner1, Marie-Aline Trotzier, Odile Filhol

  • 1Institute National de la Santé et de la Recherche Médicale, Unité Mixte de Recherche-S392, Faculté de Pharmacie, B.P. 60024, 67401 Illkirch, France.

Annals of the New York Academy of Sciences
|January 22, 2005
PubMed

Insights

Casein kinase 2 (CK2) phosphorylates the transcription factor ICBP90, regulating its antiapoptotic properties. This suggests CK2 influences cell proliferation and may be a therapeutic target in tumors expressing ICBP90.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Casein kinase 2 (CK2) is a serine/threonine kinase crucial for cell proliferation.
  • CK2 expression is frequently dysregulated in various tumors.
  • ICBP90 is a transcription factor with antiapoptotic functions and potential CK2 phosphorylation sites.

Purpose of the Study:

  • To investigate if ICBP90 serves as a substrate for CK2.
  • To elucidate the regulatory role of CK2 in ICBP90's transcriptional activity and antiapoptotic functions.

Main Methods:

  • In vitro kinase assays using purified CK2 subunits and recombinant ICBP90.
  • Analysis of ICBP90 phosphorylation by free CK2 alpha subunit versus heterotetrameric CK2.

Main Results:

  • ICBP90 is phosphorylated by CK2.
  • Phosphorylation is more efficient with the free CK2 alpha subunit compared to the heterotetrameric form.
  • CK2 activity is suggested to regulate ICBP90's transcriptional activity and antiapoptotic properties.

Conclusions:

  • CK2 acts as a regulator of ICBP90's transcriptional activity.
  • CK2-mediated phosphorylation of ICBP90 influences its antiapoptotic properties.
  • Members of the ICBP90 family may be substrates for CK2, indicating a broader role in cellular regulation.

More Related Videos

Identifying Protein-protein Interaction Sites Using Peptide Arrays07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Related Concept Videos

The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
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...
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.