Related Experiment Video

Updated: May 23, 2026

A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia
09:52

A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia

Published on: December 4, 2018

Interleukin enhancer-binding factor 3/NF110 is a target of YM155, a suppressant of survivin

Naoto Nakamura1, Tomohiro Yamauchi, Masashi Hiramoto

  • 1Drug Discovery Research, Astellas Pharma, Inc., Tsukuba, Ibaraki, 305-8585, Japan.

Molecular & Cellular Proteomics : MCP
|March 24, 2012
PubMed

Insights

The drug YM155 targets interleukin enhancer-binding factor 3 (ILF3)/NF110, a transcription factor that drives survivin expression. This interaction reveals the mechanism by which YM155 suppresses survivin, offering new insights into cancer therapy.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Pharmacology

Background:

  • Survivin is a key protein promoting cancer progression and drug resistance.
  • YM155 is known to suppress survivin expression and induce cancer cell apoptosis.
  • The precise molecular mechanism of YM155's action remains largely unelucidated.

Purpose of the Study:

  • To identify the direct molecular target of YM155 responsible for survivin suppression.
  • To elucidate the mechanism by which YM155 exerts its anti-cancer effects.
  • To investigate the role of interleukin enhancer-binding factor 3 (ILF3)/NF110 in survivin regulation and YM155 activity.

Main Methods:

  • Investigated the interaction between YM155 and the transcription factor ILF3/NF110.
  • Assessed the effect of ILF3/NF110 overexpression on survivin promoter activity.
  • Analyzed the impact of YM155 on ILF3/NF110-mediated survivin expression.
  • Characterized the binding affinity of YM155 to different regions of ILF3/NF110.

Main Results:

  • Identified ILF3/NF110 as a direct binding target of YM155.
  • Demonstrated that YM155 attenuates ILF3/NF110-enhanced survivin promoter activity in a dose-dependent manner.
  • Confirmed ILF3/NF110 as the physiological target mediating YM155's survivin suppression.
  • Showed that the C-terminal region of ILF3/NF110 is crucial for both survivin expression and high-affinity YM155 binding.

Conclusions:

  • ILF3/NF110 is the direct molecular target of YM155, mediating survivin suppression.
  • The C-terminal domain of ILF3/NF110 plays a critical role in regulating survivin expression and YM155 binding.
  • This discovery provides a mechanistic basis for YM155's therapeutic potential in cancers dependent on survivin.

More Related Videos

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice08:09

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice

Published on: March 24, 2017

Related Concept Videos

NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
NF-kB-dependent Signaling Pathway02:26

NF-kB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
Induced Pluripotent Stem Cells01:06

Induced Pluripotent Stem Cells

Stem cells are undifferentiated cells that divide and produce different cell types. Ordinarily, cells that have differentiated into a specific cell type are terminally differentiated; however, scientists have found a way to reprogram these mature cells so that they dedifferentiate and return to an unspecialized, proliferative state. These cells are pluripotent like embryonic stem cells—able to produce all cell types—and are called induced pluripotent stem cells (iPSCs).
Somatic cells are...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
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...