Related Experiment Video
Updated: May 25, 2026
07:26
Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
Published on: April 1, 2022
Phosphorylation of basic helix-loop-helix transcription factor Twist in development and disease
1Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.
Biochemical Society Transactions
|January 21, 2012
Summary
Twist, a transcription factor crucial for embryonic development, is reactivated in cancer, promoting metastasis. This review explores how phosphorylation regulates Twist activity and its role in cancer progression.
Area of Science:
- Molecular Biology
- Developmental Biology
- Cancer Biology
Background:
- The transcription factor Twist is essential for embryonic cell migration but is typically inactivated postnatally.
- Reactivation of Twist is linked to cancer progression, enabling tumor cell dissemination and metastasis.
Purpose of the Study:
- To review recent advances in understanding Twist regulation and activity.
- To focus on the role of phosphorylation in controlling Twist's function in cancer.
Main Methods:
- Literature review of recent studies on Twist regulation.
- Analysis of signaling pathways and kinases involved in Twist phosphorylation.
- Discussion of Twist's role in transducing biological signals.
Main Results:
- Phosphorylation-dependent regulation significantly impacts Twist activity.
- Specific upstream kinases modulate Twist activity, influencing its role in cancer.
- Understanding these regulatory mechanisms provides insights into Twist's function.
Conclusions:
- Phosphorylation is a key mechanism controlling Twist activity and its oncogenic functions.
- Targeting Twist phosphorylation pathways may offer therapeutic strategies for cancer.
- Further research is needed to fully elucidate the complex regulation of Twist.
More Related Videos
Related Concept Videos
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
02:54Canonical Wnt Signaling Pathway
The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...
02:54Canonical Wnt Signaling Pathway
The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
01:16TGF - 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...