Related Experiment Video

Updated: May 20, 2026

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

Receptor protein tyrosine phosphatases and cancer: new insights from structural biology

Roman M Nikolaienko1, Boadi Agyekum, Samuel Bouyain

  • 1Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO, USA.

Cell Adhesion & Migration
|July 17, 2012
PubMed

Insights

Aberrant phosphotyrosine signaling, involving receptor protein tyrosine phosphatases (RPTPs), is linked to cancer. RPTPs can act as tumor suppressors or oncogenes, depending on their function and expression levels.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Signaling

Background:

  • Aberrant phosphotyrosine signaling is a hallmark of many cancers.
  • This aberrant signaling can stem from dysregulated tyrosine kinases or tyrosine phosphatases.
  • Altered signaling pathways are frequently associated with changes in cell adhesion mediated by cell surface receptors.

Purpose of the Study:

  • To explore the dual role of receptor protein tyrosine phosphatases (RPTPs) in cancer.
  • To understand the molecular mechanisms underlying RPTPs' tumor-suppressive or oncogenic functions.
  • To leverage recent structural data for interpreting RPTPs' roles in cancer development.

Main Methods:

  • Review and integration of recent scientific literature.
  • Analysis of structural data for extracellular and intracellular regions of RPTPs.
  • Correlation of structural insights with functional roles in cancer.

Main Results:

  • Receptor protein tyrosine phosphatases (RPTPs) can act as either tumor suppressors or oncogenes.
  • Structural information elucidates how extracellular interactions inactivate RPTPs in cancer.
  • Overexpression of specific RPTPs can contribute to tumor progression.

Conclusions:

  • RPTPs play complex roles in cancer, acting as both suppressors and promoters.
  • Structural biology provides a framework for understanding RPTPs' involvement in cancer.
  • Further research into RPTPs' functions is crucial for cancer therapy development.

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

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

Related Concept Videos

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...
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...
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...
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:
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...
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...