Related Experiment Video

Updated: Jun 15, 2026

Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence
04:56

Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence

Published on: December 30, 2025

Cancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation

Peng Zhang1, Scott Becka, Sonya E L Craig

  • 1Department of Genetics, Case Western Reserve University, Cleveland, Ohio 44106, USA

Cell Communication & Adhesion
|March 17, 2010
PubMed

Insights

Mutations in protein tyrosine phosphatase rho (PTPrho) disrupt cell-cell adhesion, a key function in preventing cancer progression. This study highlights the role of fibronectin type III repeats in PTPrho

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • Protein tyrosine phosphatase rho (PTPrho) is frequently mutated in human cancers.
  • PTPrho plays a crucial role in homophilic cell-cell aggregation.
  • The extracellular region of PTPrho contains domains including MAM, immunoglobulin, and fibronectin type III (FNIII) repeats.

Purpose of the Study:

  • To evaluate the contribution of FNIII repeats to PTPrho-mediated cell-cell adhesion.
  • To investigate the impact of tumor-derived mutations in FNIII repeats on PTPrho function.

Main Methods:

  • Deletion of FNIII repeats from PTPrho.
  • Analysis of cell-cell aggregation in cells expressing wild-type and mutant PTPrho.
  • Characterization of tumor-derived mutations within the FNIII repeats.

Main Results:

  • Deletion of FNIII repeats significantly impairs PTPrho-mediated cell-cell aggregation.
  • All investigated tumor-derived mutations in the FNIII repeats disrupt PTPrho's ability to mediate cell-cell adhesion.
  • These findings complement previous studies on MAM and immunoglobulin domains.

Conclusions:

  • The FNIII repeats are essential for PTPrho's function in cell-cell adhesion.
  • Mutational inactivation of PTPrho, particularly within the FNIII repeats, may contribute to cancer progression by compromising cell adhesion.

More Related Videos

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion09:23

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion

Published on: April 2, 2020

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Cancer Cell Migration through Invadopodia01:35

Cancer Cell Migration through Invadopodia

Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...
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...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
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...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity: