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Article

The PTEN lipid phosphatase domain is not required to inhibit invasion of glioma cells.

Cancer research - 1 Nov 1999

Maier D, Jones G, Li X, Schönthal A H, Gratzl O, Van Meir E G, Merlo A

Abstract excerpt

The tumor suppressor PTEN negatively controls the phosphoinositide 3-kinase pathway for cell survival by dephosphorylating the phospholipid substrates phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. PTEN has been proposed to dephosphorylate focal adhesion kinase and is implicated in the regulation of cell spreading and motility. We analyzed the role of PTEN in invasion using...

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Share to Cell Adhesion Molecules
Share to Focal Adhesion Kinase 1
Share to Focal Adhesion Protein-Tyrosine Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10554022

Genes

PTEN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The PTEN lipid phosphatase domain is not required to inhibit invasion of glioma cells.PMID 10554022Read ↗

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Regulation of cell migration by the C2 domain of the tumor suppressor PTEN.Semantic proximity Read ↗

The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells.Semantic proximity Read ↗

Tumor suppressor PTEN: modulator of cell signaling, growth, migration and apoptosisSemantic proximity Read ↗

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