Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion.

Molecular cancer research : MCR - 1 Jul 2008

Yu Jianshi, Becka Scott, Zhang Peng, Zhang Xiaodong, Brady-Kalnay Susann M, Wang Zhenghe

Abstract excerpt

Receptor protein tyrosine phosphatase T (PTPRT/PTPrho) is frequently mutated in human cancers including colon, lung, gastric, and skin cancers. More than half of the identified tumor-derived mutations are located in the extracellular part of PTPrho. However, the functional significance of those extracellular domain mutations remains to be defined. Here we report that the extracellular domain of PTPrho mediates...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Adhesion
Share to Cell Aggregation
Share to Extracellular Space

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoglobulins

Share to Insecta

Share to Neoplasms

Share to Protein Structure, Tertiary

Share to Receptor-Like Protein Tyrosine Phosphatases, Class 2

Source

Open in PubMed Open full text

Identifiers

PMID: 18644975
DOI: 10.1158/1541-7786.MCR-07-2123
PMCID: PMC2614372

Genes

PTPRT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion.PMID 18644975Read ↗

Cancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation.Semantic proximity Read ↗

Receptor protein tyrosine phosphatases and cancer: new insights from structural biology.Semantic proximity Read ↗

Tumour suppressor function of protein tyrosine phosphatase receptor-T.Semantic proximity Read ↗

Mutational analysis of the tyrosine phosphatome in colorectal cancers.Semantic proximity Read ↗

RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.Semantic proximity Read ↗

Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T.Semantic proximity Read ↗

EGFR regulates RhoA-GTP dependent cell motility in E-cadherin mutant cells.Semantic proximity Read ↗

Disrupting the Transmembrane Domain Oligomerization of Protein Tyrosine Phosphatase Receptor J Promotes its Activity in Cancer CellsSemantic proximity Read ↗

PTPRK negatively regulates transcriptional activity of wild type and mutated oncogenic beta-catenin and affects membrane distribution of beta-catenin/E-cadherin complexes in cancer cells.Semantic proximity Read ↗

Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain.Semantic proximity Read ↗

Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis.Semantic proximity Read ↗

The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.