ArticleMolecular biology of the cell2012
The inositol 5-phosphatase SHIP2 is an effector of RhoA and is involved in cell polarity and migration.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 54 citations in OpenAlex.
- The power of five - inositol polyphosphate 5-phosphatase gene mutations at the intersection of development and disease.FEBS letters · 2026Review
- SHIP2-PLK1 crosstalk promotes sensitivity to dual inhibition in esophageal squamous cell carcinoma.Molecular cancer · 2025Article
- The Protein Kinase aPKC as Well as the Small GTPases RhoA and Cdc42 Regulates Neutrophil Chemotaxis Partly by Recruiting the ROCK Kinase to the Leading Edge.Genes to cells : devoted to molecular & cellular mechanisms · 2025Article
- Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2.Structure (London, England : 1993) · 2024Article
- PHB2 promotes SHIP2 ubiquitination via the E3 ligase NEDD4 to regulate AKT signaling in gastric cancer.Journal of experimental & clinical cancer research : CR · 2024Article
- Enhancement of Phosphorylation and Transport Activity of the Neuronal Glutamate Transporter Excitatory Amino Acid Transporter 3 by C3bot and a 26mer C3bot Peptide.Frontiers in cellular neuroscience · 2022Article
- PKCε regulates Rho GTPases and actin cytoskeleton reorganization in non-small cell lung cancer cells.Small GTPases · 2021Article
- PTEN and Other PtdIns(3,4,5)PInternational journal of molecular sciences · 2020Review
- IQGAP2 Inhibits Migration and Invasion of Gastric Cancer Cells via Elevating SHIP2 Phosphatase Activity.International journal of molecular sciences · 2020Article
- The impact of phosphoinositide 5-phosphatases on phosphoinositides in cell function and human disease.Journal of lipid research · 2019Review
- Solution structure of SHIP2 SH2 domain and its interaction with a phosphotyrosine peptide from c-MET.Archives of biochemistry and biophysics · 2018Article
- Tumor Cell Invadopodia: Invasive Protrusions that Orchestrate Metastasis.Trends in cell biology · 2017Review
- Optogenetic activation of Plexin-B1 reveals contact repulsion between osteoclasts and osteoblasts.Nature communications · 2017Article
- INPPL1 gene mutations in opsismodysplasia.Journal of human genetics · 2017Review
- PI3K/SHIP2/PTEN pathway in cell polarity and hepatitis C virus pathogenesis.World journal of hepatology · 2017Review
- Quantitative GTPase Affinity Purification Identifies Rho Family Protein Interaction Partners.Molecular & cellular proteomics : MCP · 2017Article
- Lipid phosphatase SHIP2 functions as oncogene in colorectal cancer by regulating PKB activation.Oncotarget · 2016Article
- Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt.Journal of gastroenterology · 2016Article
- Rabphilin-3A as a Targeted Autoantigen in Lymphocytic Infundibulo-neurohypophysitis.The Journal of clinical endocrinology and metabolism · 2015Article
- The PI3K/Akt signaling pathway exerts effects on the implantation of mouse embryos by regulating the expression of RhoA.International journal of molecular medicine · 2014Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell migration is essential for various physiological and pathological processes. Polarization in motile cells requires the coordination of several key signaling molecules, including RhoA small GTPases and phosphoinositides. Although RhoA participates in a front-rear polarization in migrating cells, little is known about the functional interaction between RhoA and lipid turnover. We find here that src-homology 2-containing inositol-5-phosphatase 2 (SHIP2) interacts with RhoA in a GTP-dependent manner. The association between SHIP2 and RhoA is observed in spreading and migrating U251 glioma cells. The depletion of SHIP2 attenuates cell polarization and migration, which is rescued by wild-type SHIP2 but not by a mutant defective in RhoA binding. In addition, the depletion of SHIP2 impairs the proper localization of phosphatidylinositol 3,4,5-trisphosphate, which is not restored by a mutant defective in RhoA binding. These results suggest that RhoA associates with SHIP2 to regulate cell polarization and migration.
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