Related Experiment Video

Updated: Aug 10, 2026

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia
10:49

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia

Published on: September 19, 2013

Abl tyrosine kinase in signal transduction and cell-cycle regulation

J Y Wang1

  • 1Department of Biology and Center for Molecular Genetics, University of California, San Diego 92093-0116.

Current Opinion in Genetics & Development
|February 1, 1993
PubMed

Insights

The biological role of c-Abl tyrosine kinase is unclear, but new discoveries point to its F-actin and DNA-binding domains being crucial for its function. Deleting these domains in mice eliminates biological activity, suggesting c-Abl regulates processes involving F-actin and DNA.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The precise biological function of the c-Abl tyrosine kinase is not fully understood.
  • Recent research has uncovered novel domains within c-Abl, offering new insights into its potential roles.

Purpose of the Study:

  • To investigate the biological function of c-Abl tyrosine kinase.
  • To explore the significance of newly discovered domains in c-Abl's activity.

Main Methods:

  • Discovery of an F-actin binding domain in c-Abl.
  • Identification of a sequence-specific DNA-binding domain in c-Abl.
  • Demonstration of cell-cycle-regulated DNA binding by c-Abl.

Main Results:

  • Deletion of the F-actin and DNA-binding domains in mouse c-Abl resulted in a loss of biological function.
  • Despite domain deletion, the tyrosine kinase remained active, indicating the domains are essential for specific biological roles.
  • c-Abl's DNA binding capability is regulated by the cell cycle.

Conclusions:

  • The F-actin and DNA-binding domains are critical for the biological function of c-Abl.
  • c-Abl tyrosine kinase likely plays a regulatory role in processes involving F-actin and specific DNA elements.
  • Further research into these domains may elucidate the complete biological function of c-Abl.

More Related Videos

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays07:42

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants07:38

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

Related Concept Videos

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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include: