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Article

Phospholipid-binding sites of phosphatase and tensin homolog (PTEN): exploring the mechanism of phosphatidylinositol 4,5-bisphosphate activation.

The Journal of biological chemistry - 16 Jan 2015

Wei Yang, Stec Boguslaw, Redfield Alfred G, Weerapana Eranthie, Roberts Mary F

Abstract excerpt

The lipid phosphatase activity of the tumor suppressor phosphatase and tensin homolog (PTEN) is enhanced by the presence of its biological product, phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). This enhancement is suggested to occur via the product binding to the N-terminal region of the pro...

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Identifiers

PMID: 25429968
DOI: 10.1074/jbc.M114.588590
PMCID: PMC4340405

Genes

PTEN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25429968-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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Phospholipid-binding sites of phosphatase and tensin homolog (PTEN): exploring the mechanism of phosphatidylinositol 4,5-bisphosphate activation.PMID 25429968Read ↗

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Elucidating PTEN conformational dynamics and phosphatase regulation via integrative modeling and mutation prediction.Semantic proximity Read ↗

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