ArticleBiochemical and biophysical research communications2013
Determinants of the tumor suppressor INPP4B protein and lipid phosphatase activities.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Targeting SHP2 with an Active Site Inhibitor Blocks Signaling and Breast Cancer Cell Phenotypes.ACS bio & med chem Au · 2023Article
- Role of inositol polyphosphate-4-phosphatase type II in oncogenesis of digestive system tumors.World journal of gastrointestinal oncology · 2023Review
- INPP4B protects from metabolic syndrome and associated disorders.Communications biology · 2021Article
- Novel Small-Molecule Inhibitor for the Oncogenic Tyrosine Phosphatase SHP2 with Anti-Breast Cancer Cell Effects.ACS omega · 2020Article
- Deletion of inositol polyphosphate 4-phosphatase type-II B affects spermatogenesis in mice.PloS one · 2020Article
- Inositol polyphosphate 4-phosphatase type II regulation of androgen receptor activity.Oncogene · 2019Article
- INPP4B promotes cell survival via SGK3 activation in NPM1-mutated leukemia.Journal of experimental & clinical cancer research : CR · 2018Article
- Regulation of PI3K effector signalling in cancer by the phosphoinositide phosphatases.Bioscience reports · 2017Review
- INPP4B is an oncogenic regulator in human colon cancer.Oncogene · 2016Article
- INPP4B suppresses prostate cancer cell invasion.Cell communication and signaling : CCS · 2014Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The tumor suppressor INPP4B is an important regulator of phosphatidyl-inositol signaling in the cell. Reduced INPP4B expression is associated with poor outcomes for breast, prostate, and ovarian cancer patients. INPP4B contains a CX5R catalytic motif characteristic of dual-specificity phosphatases, such as PTEN. Lipid phosphatase activity of INPP4B has previously been described. In this report we show that INPP4B can dephosphorylate para-nitrophenyl phosphate (pNPP) and 6,8-difluoro-4-methylumbelliferyl (DiFMUP), synthetic phosphotyrosine analogs, suggesting that INPP4B has protein tyrosine phosphatase (PTP) activity. Using mutagenesis, we examined the functional role of specific amino acids within the INPP4B C842KSAKDR catalytic site. The K843M mutant displayed increased pNPP hydrolysis, the K846M mutant lost lipid phosphatase activity with no effect on PTP activity, and the D847E substitution ablated PTP activity and significantly reduced lipid phosphatase activity. Further, we show that INPP4B but not PTEN is able to reduce tyrosine phosphorylation of Akt1 and both the lipid and PTP activity of INPP4B likely contribute to the reduction of Akt1 phosphorylation. Taken together our data identified key residues in the INPP4B catalytic domain associated with lipid and protein phosphatase activities and found a robust downstream target regulated by INPP4B but not PTEN.
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