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

The tumor suppressor PP2A Abeta regulates the RalA GTPase.

Cell - 1 Jun 2007

Sablina Anna A, Chen Wen, Arroyo Jason D, Corral Laura, Hector Melissa, Bulmer Sara E, DeCaprio James A, Hahn William C

Abstract excerpt

The serine-threonine protein phosphatase 2A (PP2A) is a heterotrimeric enzyme family that regulates numerous signaling pathways. Biallelic mutations of the structural PP2A Abeta subunit occur in several types of human tumors; however, the functional consequences of these cancer-associated PP2A Abeta mutations in cell transformation remain undefined. Here we show that suppression of PP2A Abeta expression permits...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Cell Line
Share to Cell Transformation, Neoplastic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genes, Tumor Suppressor

Share to Lung Neoplasms

Share to Neoplasm Proteins

Share to Phosphorylation

Share to Protein Phosphatase 2

Source

Open in PubMed Open full text

Identifiers

PMID: 17540176
DOI: 10.1016/j.cell.2007.03.047
PMCID: PMC1945132

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

The tumor suppressor PP2A Abeta regulates the RalA GTPase.PMID 17540176Read ↗

Mutagenesis and expression of the scaffolding Aalpha and Abeta subunits of PP2A: assays for measuring defects in binding of cancer-related Aalpha and Abeta mutants to the regulatory B and catalytic C subunits.Semantic proximity Read ↗

The role of PP2A A subunits in tumor suppression.Semantic proximity Read ↗

PPP2R1B gene alterations inhibit interaction of PP2A-Abeta and PP2A-C proteins in colorectal cancers.Semantic proximity Read ↗

LKB1 catalytic activity contributes to estrogen receptor alpha signaling.Semantic proximity Read ↗

Ral GTPases and cancer: linchpin support of the tumorigenic platform.Semantic proximity Read ↗

Reduced expression of the Aalpha subunit of protein phosphatase 2A in human gliomas in the absence of mutations in the Aalpha and Abeta subunit genes.Semantic proximity Read ↗

Aurora-A phosphorylates, activates, and relocalizes the small GTPase RalA.Semantic proximity Read ↗

The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation.Semantic proximity Read ↗

RACK1 stabilises the activity of PP2A to regulate the transformed phenotype in mammary epithelial cells.Semantic proximity Read ↗

Essential Role of Cdc42 in Ras-Induced Transformation Revealed by Gene TargetingSemantic proximity Read ↗

Protein phosphatase 1alpha activity prevents oncogenic transformation.Semantic proximity Read ↗

Biochemical characterization of yeast RAS2 mutants reveals a new region of ras protein involved in the interaction with GTPase-activating proteins.Semantic proximity Read ↗

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