Related Experiment Video

Updated: Oct 10, 2025

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.3K

Protein Tyrosine Phosphatases: Mechanisms in Cancer

Vignesh Sivaganesh1,2, Varsha Sivaganesh1, Christina Scanlon1

  • 1Department of Biological Sciences, University of the Sciences, 600 S 43rd St, Philadelphia, PA 19104, USA.

International Journal of Molecular Sciences
|December 10, 2021
PubMed

Insights

Protein tyrosine phosphatases (PTPs) are emerging cancer targets, acting as both tumor suppressors and oncogenes. This review explores key PTPs and their dual roles in cancer progression and suppression.

Area of Science:

  • Oncology
  • Biochemistry
  • Molecular Biology

Background:

  • Receptor tyrosine kinases are established cancer drug targets.
  • Protein tyrosine phosphatases (PTPs) are increasingly recognized as critical regulators in cancer.
  • PTPs historically viewed as negative regulators of tyrosine kinases, now understood to have dual roles.

Purpose of the Study:

  • To review key protein tyrosine phosphatases investigated in various cancers.
  • To explore the mechanisms by which PTPs promote or suppress cancer.
  • To highlight PTPs as emerging therapeutic targets in oncology.

Main Methods:

  • Literature review of PTPs in cancer research.
  • Analysis of PTP roles as tumor suppressors and oncogenes.
  • Examination of molecular mechanisms underlying PTP function in cancer.

Main Results:

  • Identified key PTPs with significant roles in diverse cancer types.
  • Elucidated distinct mechanisms for pro-cancerous and anti-cancerous PTP activities.
  • Demonstrated the complex and context-dependent functions of PTPs in tumorigenesis.

Conclusions:

  • PTPs represent a significant and emerging class of therapeutic targets in cancer treatment.
  • Understanding PTPs' dual roles is crucial for developing effective cancer therapies.
  • Targeting specific PTPs offers potential for novel anti-cancer strategies.
Keywords:
PTPbreast cancergastric canceroncogeneprostate cancerprotein tyrosine kinaseprotein tyrosine phosphatasereceptor tyrosine kinasetumor suppressor

More Related Videos

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases06:56

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

Published on: September 6, 2024

492
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

2.5K

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...
13.7K
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...
3.9K
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...
13.3K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
6.6K
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:
3.1K
Phosphorylation01:02

Phosphorylation

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...
52.0K